Information on EC 3.1.22.4 - crossover junction endodeoxyribonuclease

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
3.1.22.4
-
RECOMMENDED NAME
GeneOntology No.
crossover junction endodeoxyribonuclease
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction)
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
P0AG74
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphoric ester
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A22 resolvase
-
-
A22R protein
-
-
Ape-Hjc
Q9YEX2
-
BpuJI
-
BpuJI is cleaved into a N-terminal domain, NTD, binding domain, and a C-terminal domain, CTD, catalytic domain, CTD is structurally related to archaeal Holliday junction resolvases
crossover junction endodeoxyribonuclease
-
-
-
-
crossover junction endodeoxyribonuclease
-
-
crossover junction endodeoxyribonuclease
-
-
crossover junction endodeoxyribonuclease
-
-
crossover junction endodeoxyribonuclease
-
-
crossover junction endodeoxyribonuclease
-
-
crossover junction endodeoxyribonuclease
-
-
cruciform-cutting endonuclease
-
-
-
-
ECRuvC protein
-
-
Eme1
-
subunits of nuclear Holliday junction resolvase
endonuclease Hje
-
-
endonuclease RuvC
-
-
-
-
endonuclease VII
-
-
endonuclease VII
P13340
-
endonuclease VII resolvase
-
-
endonuclease X3
-
-
-
-
FPV resolvase
-
-
GEN1
-
-
GEN1 protein
-
-
HJ resolvase
-
-
HJ resolvase
-
-
HJ resolvase
-
-
HJ resolvase
-
-
HJ resolvase
-
-
HJ resolvase
-
-
hjc holliday junction resolvase
-
-
Hjc protein
Q9V301
-
Hjc protein
Q97YX6
-
Hjc protein
Q9UWX8
-
Hjc protein
Q97YX6
-
-
Hjc resolvase
-
-
Hje endnuclease
-
-
Hje endonuclease
-
-
Hjr protein
-
-
Holliday juction resolvase ruvC
-
-
-
-
Holliday junction endonuclease
-
-
Holliday junction endonuclease CCE1
-
-
-
-
Holliday junction nuclease ruvC
-
-
-
-
Holliday junction resolvase
-
-
-
-
Holliday junction resolvase
-
-
Holliday junction resolvase
-
-
Holliday junction resolvase
-
-
Holliday junction resolvase
-
-
Holliday junction resolvase
-
-
Holliday junction resolvase
-
-
Holliday junction resolvase
-
-
-
Holliday junction resolvase
-
-
Holliday junction resolvase
-
-
Holliday junction resolvase
-
-
holliday junction resolvase hjc
-
-
Holliday junction resolvase RusA
-
-
Holliday junction resolvase SpCCE1
-
-
Holliday junction resolvase Ydc2
-
-
Holliday junction resolving enzyme
-
-
Holliday junction resolving enzyme
-, Q9V301
-
Holliday junction resolving enzyme
-
-
Holliday junction resolving enzyme
Q97YX6
-
Holliday junction resolving enzyme
Q97YX6
-
-
Holliday junction resolving enzyme Hjc
-
-
Holliday junction resolving enzyme Hjc
-
-
-
Holliday junction resolving enzyme Hje
-
-
Holliday junction resolving enzyme Hje
-
-
-
Holliday junction resolving enzyme Hjr
-
-
Holliday junction-cleaving endonuclease
-
-
-
-
Holliday junction-resolving endoribonuclease
-
-
-
-
Holliday junction-resolving enzyme
-
-
Holliday junction-resolving enzyme Cce1
-
-
Holliday junction-resolving enzyme Hjc
-
-
Holliday junction-resolving enzymes
Q9YEX2
-
Holliday junction-resolving enzymes
Q9V0H1
-
Holliday junction-resolving enzymes
-
-
mammalian HJ resolvase
-
-
Mus81
-
subunit of nuclear Holliday junction resolvase
Mus81 endonuclease
-
-
Mus81 endonuclease
-
Mus81 is the catalytic component of the heterodimeric endonuclease Mus81-Eme1
MUS81 endonuclease complex
-
-
Mus81 nuclease
-
-
Mus81 nuclease
-
-
Mus81-Eme1
-
-
Mus81-Eme1
-
-
Mus81-Eme1 endonuclease
-
-
Mus81-Eme1 endonuclease complex
-
-
MUS81-EME1A complex
-
cleaves 3'-flap structures, nicked Holliday junctions, and, with reduced efficiency, intact Holliday junctions
MUS81-EME1B complex
-
cleaves 3'-flap structures, nicked Holliday junctions, and, with reduced efficiency, intact Holliday junctions
Mus81-Mms4 endonuclease
-
-
Mus81-Mms4/Eme1 endonuclease
-
-
Mus81.Eme1 Holliday junction resolvase
-
-
Mus81/Mms4 complex
-
-
Pab-Hjc
Q9V0H1
-
phage T7 endonuclease I
-
-
phage T7 junction-resolving enzyme endonuclease I
-
-
RecU endonuclease
-
-
RecU HJ resolvase
Q49422
-
RecU HJ resolvase
Q49422
-
-
RecU Holliday junction resolvase
-
-
RecU Holliday junction resolvase
-
a ruvC functional analog
RecU Holliday junction resolvase
Bacillus subtilis BG633
-
a ruvC functional analog
-
RecU Holliday junction resolvase
-
-
RecU Holliday junction resolvase
Q49422
-
RecU Holliday junction resolvase
Q49422
-
-
RecU Holliday-junction resolvase
-
-
RecU Holliday-junction resolvase
Bacillus subtilis YB886
-
-
-
RecU protein
-
-
RecU protein
-
-
-
RecU resolvase
-
-
RecUMge
Q49422
gene name
RecUMge
Q49422
gene name
-
resolvase
-
-
Resolvase of Telomeres
-
-
resolvase SIRV2
-
-
resolving enzyme CCE1
-
-
-
-
resolving enzyme CCE1
-
-
restriction endonuclease
-
-
RusA endonuclease
-
-
-
-
RusA Holliday junction resolvase
-
-
-
-
RusA Holliday junction resolvase
-
-
RusA Holliday junction resolvase
-
the enzyme is encoded by a cryptic rusA gene of the defective pyrophage DLP12
RuvA
-
RuvA is a Holliday junction-specific DNA-binding protein and facilitates the interaction of RuvB with the junction
ruvABC
Bacillus subtilis BG633
-
-
-
RuvABC complex
-
resolves Holliday junctions to produce recombinant molecules
RuvC endonuclease
-
-
-
-
RuvC Holliday junction resolvase
-
-
RuvC junction resolvase
-
-
RuvC resolvase
-
-
SpCCe1 Holliday junction resolvase
-
-
T4 endo VII resolvase
-
-
T4 endonuclease VII
-
-
T4 gp49 endonuclease VII resolvase
-
-
T7 endonuclease I
-
-
telomere resolvase
-
-
TRF2
-
-
TTAGGG repeat factor 2
-
-
additional information
-
the enzyme belongs to the nuclease superfamily, and is clearly related to the restriction enzymes
additional information
-
GEN1 is a member of the Rad2/XPG nuclease family
CAS REGISTRY NUMBER
COMMENTARY
99676-43-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain BG633, BG501, BG651, DK53, DK54, DK55, DK56
-
-
Manually annotated by BRENDA team
strain YB886
-
-
Manually annotated by BRENDA team
Bacillus subtilis BG633
strain BG633, BG501, BG651, DK53, DK54, DK55, DK56
-
-
Manually annotated by BRENDA team
Bacillus subtilis YB886
strain YB886
-
-
Manually annotated by BRENDA team
the enzyme RusA resolvase is encoded by a cryptic rusA gene of the defective pyrophage DLP12
-
-
Manually annotated by BRENDA team
several strains
-
-
Manually annotated by BRENDA team
cell lines irs3, irs1, irs1SF and V79
-
-
Manually annotated by BRENDA team
gene MG352
-
-
Manually annotated by BRENDA team
gene RecUMge
UniProt
Manually annotated by BRENDA team
gene RecUMge
UniProt
Manually annotated by BRENDA team
no activity in mammalia
-
-
-
Manually annotated by BRENDA team
different strains
-
-
Manually annotated by BRENDA team
fission yeast
-
-
Manually annotated by BRENDA team
fission yeast
-
-
Manually annotated by BRENDA team
Spcce1:ura4+ insertion mutant strain devoid of the Holliday junction resolvase activity
-
-
Manually annotated by BRENDA team
pox virus family
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
yen1DELTA mutants are repair-proficient. Yen1DELTA mus81ELTA double mutant displays a more severe repair-defective phenotype than the mus81DELTA mutant. Yen1DELTA cells do not exhibit any obvious sensitivity to DNA-damaging agents like the wild-type, whereas yen1DELTA mus81DELTA double mutants are exquisitely sensitive to a variety of DNA-damaging agents that disturb replication fork progression. Yen1DELTA mus81DELTA cells show a hypersensitivity to all agents for which the mus81DELTA single mutant is sensitive: hydroxyurea, 4-nitroquinoline 1-oxide, phleomycin, camptothecin, UV-light, nitrogen mustard and cisplatin. Neither the yen1DELTA or mus81DELTA single mutants nor the yen1DELTA mus81DELTA double mutant show any sensitivity to ionizing radiation up to 200 Gy. Yen1DELTA sgs1DELTA cells are viable and exhibit a similar methyl methanesulfonate, hydroxyurea and 4-nitroquinoline 1-oxide-sensitivity to that observed with the sgs1DELTA single mutant. Toxic recombination intermediates accumulate in the absence of Yen1 and Mus81. After methyl methanesulfonate treatment, yen1DELTA mus81DELTA double mutants arrest with a G2 DNA content and unsegregated chromosomes. Overexpression of Yen1 partially rescues the methyl methanesulfonate sensitivity of mus81DELTA, Yen1 is the only member of the Rad2 family of nucleases that can complement mus81 defects. Yen1ELTA mus81ELTA double mutants are synthetically sick: 15-20 min increase in the duration of the cell cycle of yen1DELTA mus81DELTA double mutants compared with wild-type, yen1DELTA or mus81DELTA cells growing in YPD. Constitutive expression of Yen1-3xHA, but not the catalytically dead version of Yen1, reduces the doubling time of the yen1DELTA mus81DELTA mutant to wild-type levels
malfunction
-
single mutants of hjc and hef display no significant defects in growth or homologous recombination. Deletion of hef confers only moderate sensitivity to DNA crosslinking agents, whereas mutation of FANCM in leads to hypersensitivity in eukaryotes. Absence of hef or hjc leads to growth defects in presence of mitomycin C, deletion of both leads to synthetic lethality
malfunction
-
strains lacking RuvABC are inviable and accumulate Holliday junctions that interfere with growth and division of the cells
malfunction
-
yeast strains deleted for both YEN1 and MMS4 show a reduction in growth rate, and are very sensitive to DNA-damaging agents. Yeast cells are unable to carry out meiosis in the absence of both resolvases
malfunction
-
gen-1 mutants are defective in DNA damage-dependent cell cycle arrest and apoptosis and in positional cloning of GEN-1, phenotypes, detailed overview
metabolism
-
gen-1 acts in a non-canonical DNA damage checkpoint pathway
physiological function
Q9V301
the enzyme is involved in the pathway for homologous recombination of the cellular genome, which includesthe RadA protein for strand exchange, and the Hjc protein for junction resolution
physiological function
Q97YX6, -
the enzyme is involved in the pathway for homologous recombination of the cellular genome, which includes the RadA protein for strand exchange, and the Hjc protein for junction resolution
physiological function
-
Yen1 and Mus81-Mms4 provide alternative and/or overlapping pathways for the repair of methyl methanesulfonate-induced DNA lesions. Yen1 can act upon recombination/repair intermediates that arise in MUS81-defective cells following replication fork damage
physiological function
-
four-way DNA Holliday junctions are resolved into duplex species by the action of the junction-resolving enzymes, nucleases selective for the structure of helical branchpoints. Mechanism of structural selectivity of these enzymes, overview
physiological function
-
Hef, a XPF/MUS81 family member found in Euryarchaea and is related to the Fanconi anemia protein FANCM, is essential for cell viability when the Holliday junction resolvase Hjc is absent, and both the helicase and nuclease activities of Hef are indispensable. Hef and Hjc provide alternative means to restart stalled DNA replication forks
physiological function
-
Holliday junction resolution is essential for chromosome segregation at meiosis and the repair of stalled/collapsed replication forks in mitotic cells. Resolution by introduction of symmetrically related nicks in two strands at, or close to, the junction point. Structural basis and mechanism of Holliday junction resolution by the human GEN1 protein, overview
physiological function
-
RuvABC resolves Holliday junctions, with RuvAB driving branch migration and RuvC catalyzing junction cleavage
physiological function
-
in vivo the T4 phage packaging motor deals with Y- or X-structures in the replicative concatemer substrate by employing a portal-bound Holliday junction resolvase that trims and releases these DNA roadblocks to packaging. Purified T4 gp49 endonuclease VII resolvase can release DNA compression in vitro in prohead portal packaging motor anchored and arrested Y-DNA substrates. Conformational changes in both the motor proteins and the DNA substrate itself that are associated with the power stroke of the motor are consistent with a proposed linear motor employing a terminal-to-portal DNA grip-and-release mechanism
physiological function
-
poxvirus DNA replication generates linear concatemers containing many copies of the viral genome with inverted repeat sequences at the junctions between monomers. The inverted repeats refold to generate Holliday junctions, which are cleaved by the virus-encoded resolvase enzyme to form unit-length genomes
physiological function
-
the RecU protein has two activities: to recognize, distort, and cleave four-stranded recombination intermediates and to modulate RecA activities. The RuvB interaction and the catalytic residues are located in the cap region of dimeric RecU, while the stalk region is essential not only for RecA modulation but also for Holliday junction recognition
physiological function
-
the Sgs1-Top3-Rmi1 complex constitutes the main pathway for the processing of Holliday junction-containing homologous recombination repair intermediates but that Mus81-Mms4 can also resolve these intermediates. These intermediates are slowly resolved at the restrictive temperature, revealing a redundant resolution activity when Rmi1 is impaired. This resolution depends on Mus81-Mms4 but not on either Slx1-Slx4 or another HJ resolvase, Yen1
physiological function
Q49422
RecUMge is a Holliday junction resolvase that may play a central role in recombination in Mycoplasma genitalium
physiological function
-
Holliday junctions need to be resolved to allow chromosome segregation, they are formed during homologous recombination. Both Yen1 and Mms4/Mus81 play important but not identical roles during vegetative growth and in meiosis. Yen1 and Mms4/Mus81 act as alternative resolvases for recombination events in meiosis, and the activity of at least one of them is essential to ensure proper meiosis and sporulation
physiological function
-
identification of a Caenorhabditis elegans dual function DNA double-strand break repair and DNA damage signaling protein orthologous to the human GEN1 Holliday junction resolving enzyme. GEN-1 is required for DNA double-strand break repair. The DNA damage-signaling function of GEN-1 is separable from its role in DNA repair. GEN-1 promotes germ cell cycle arrest and apoptosis via a pathway that acts in parallel to the canonical DNA damage response pathway mediated by RPA loading, CHK1 activation, and CEP-1/p53-mediated apoptosis induction. GEN-1 acts redundantly with the 9-1-1 complex to ensure genome stability. GEN-1 might act as a dual function Holliday junction resolvase that may coordinate DNA damage signaling with a late step in DNA double-strand break repair
physiological function
-
molecular mechanism for the Holliday junction resolving enzyme four-way junction cleavage bias, minimal requirements for four-way junction cleavage, and substrate specificity. The cleavage is specific to four-way DNA junctions and inactive on other branched DNA molecules
physiological function
-
RecUMge is a Holliday junction resolvase that may play a central role in recombination in Mycoplasma genitalium
-
physiological function
-
the enzyme is involved in the pathway for homologous recombination of the cellular genome, which includes the RadA protein for strand exchange, and the Hjc protein for junction resolution
-
metabolism
-
Holliday junction resolving enzyme is a key enzyme in SIRV2 genome replication. Modeling linking SIRV2 Holliday junction resolving enzyme genome resolution to viral particle assembly, overview
additional information
-
recognition and manipulation of junction structure, overview. Model of DNA bound in the active site of phage T7 endonuclease I
additional information
-
recognition and manipulation of junction structure, overview
additional information
-
GEN1 is a monomeric 5'-flap endonuclease. The unique feature of GEN1 that distinguishes it from other Rad2/XPG nucleases is its ability to dimerize on Holliday junctions
additional information
-
the RegG pathway is no alternative to the RuvABC pathway for resoling Holliday junctions, since the RecG pathway is very ineffective at removing junctions. A major function of RecG is to curb potentially pathological replication initiated via PriA protein at sites remote from oriC
additional information
Q49422
Holliday junction resolution by RecUMge is Mn2+-, pH- and temperature-dependent
additional information
-
Holliday junction resolution by RecUMge is Mn2+-, pH- and temperature-dependent
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3'-flapped junction in DNA + H2O
?
show the reaction diagram
-
-
-
-
?
D-loop junction in DNA + H2O
?
show the reaction diagram
-
-
-
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
-
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
-
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
-
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
-
-
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
-
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
-
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
-
-
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
at low concentrations the enzyme binds preferentially to the junction, in high concentrations it binds nonspecifically to any part of the DNA, DNA topology rather than a sequence determine the cleavage site
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
DNA topology rather than a sequence determine the cleavage site
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
nicks the ssDNA strands across the junction at symmetrical positions within the homologous arms
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
nicks the ssDNA strands across the junction at symmetrical positions within the homologous arms
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
nicks the ssDNA strands across the junction at symmetrical positions within the homologous arms
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
nicks the ssDNA strands across the junction at symmetrical positions within the homologous arms
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
sequence specific: 5'- ATT - cleavage site - G-3', substrate: homologous core of 12 bp between the arms is required for cleavage but not for binding of the enzyme to the substrate, cleaves also Y-junctions with homologous core
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
nicks favorably the continous strand at the point of strand exchange, binds to the X-junction in two specific complexes I and II, unfolds the stacked X-structure, cleaves at a subset of 5'-CT and 5'-TT sequences
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
introduces paired nicks into opposing continous strands of a stacked X-junction, independent of local sequence, cleaves an Y-junction in the presence of a bulge in one strand so that stacking of the junction becomes possible
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
Endo X3 cleaves Y-junctions,heteroduplex-loop DNA and VFS-DNA
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
performs 2 separate strand cleavages on the junction, cleaves a number of other structures that have in common bent helices
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
prefers cruciform base of X-junctions, Y-junctions are cleaved with a 5fold reduced efficiency, symmetric 6-bp sequence is needed
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
sequence specificity: cleavage 5' of a CC-dinucleotide, binds weakly to linear duplex DNA
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
under physiological levels of salt it favors X-junctions, cleaves in vitro a range of other DNAs as Y-junction, flap, flayed, nicked, partial duplex, cleavage site always 3' of thymine nucleotides, at or one nucleotide 3' from the point of strand exchange
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
cleaves at the recognition sequence 5'-CT, preference for the point of strand exchange of fixed junctions
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
optimal sequence for cleavage: A equally well as T - TT - cutting site- C better than G or A, fastest when cleavage occurs at point of strand exchange, cleavage still possible 1 nucleotide 3' of this position when directed by the sequence, Y-junctions containing the sequence are cleavable
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
specifically cleaves Holliday junctions, e.g. in bacteriophage G4 figure-8 molecules, cleavage at either of two sites present in the stem of the cruciform, not at the end of the stem
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
cleavage at or near the point of strand exchange
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
digestion of Bowtie junctions, Holliday junctions analogue containing 5',5' and 3',3' linkages in its crossover strands. The enzyme cleaves antiparralel junctions much more efficiently than parallel junctions where the protein can bind only one site at a time. The presence of two binding sites leads to communication between the two subunits of the enzyme to increase its activity
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
the enzyme makes sequential cleavages in DNA junctions within the lifetime of the complex. The cleavage at a given site is accelerated by a factor of 5-10 when it occurs subsequently to the initial cleavage, thereby facilitating productive paired resolution cleavages
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
the enzyme is required for meiotic crossing over but not for gene conversion
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
the enzyme prevents mitochondrial DNA aggregation in Schizosaccharomyces pombe
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-, Q9V301
synthetic mobile four way junction Jbm5 as a substrate. The Hjc activity cleaves all four strands of the junction, three nucleotides 3' of the point of strand exchange. Pyrococcus has two Holliday junction resolving enzymes with different specificity: the cellular Hjc enzyme, and in addition the Hjr enzyme (probably of viral origin)
-
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
Q97YX6, -
synthetic mobile four way junction Jbm5 as a substrate. The Hjc activity cleaves all four strands of the junction, three nucleotides 3' of the point of strand exchange. Sulfolobus solfataricus has two Holliday junction resolving enzymes with different specificity: the cellular Hjc enzyme, and in addition the Hjr enzyme (probably of viral origin)
-
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-, Q9V301
synthetic mobile four way junction Jbm5 as a substrate. The Hjr enzyme cleaves all four arms of the junction significantly. Cleavage occurs one nucleotide 3' of the point of strand exchange. The organisms has two Holliday junction resolving enzymes with different specificity: the cellular Hjc enzyme, and in addition the Hjr enzyme (probably of viral origin)
-
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
Q97YX6, -
synthetic mobile four way junction Jbm5 as a substrate. The Hjc activity cleaves all four strands of the junction, three nucleotides 3' of the point of strand exchange. Sulfolobus solfataricus has two Holliday junction resolving enzymes with different specificity: the cellular Hjc enzyme, and in addition the Hjr enzyme (probably of viral origin)
-
-
?
DNA + H2O
?
show the reaction diagram
-
-
-
-
?
DNA + H2O
?
show the reaction diagram
-
32P-labeled four-way DNA junction J1 or junction Z1
-
?
DNA + H2O
?
show the reaction diagram
-, Q9V301
a fixed junction with heterologous arms and a defined point of strand exchange. Holliday junction resolving enzyme Hjc cleaves all four strands of the junction, three nucleotides 3' of the point of the strand exchange. Holliday junction resolving enzyme Hjr cleaves all four arms of the junction. Significant cleavage occurs one nucleotide 3' of the point of strand exchange
-
?
DNA + H2O
?
show the reaction diagram
Q97YX6, -
a fixed junction with heterologous arms and a defined point of strand exchange. Holliday junction resolving enzyme Hjccleaves all four strands of the junction, three nucleotides 3' of the point of the strand exchange. Holliday junction resolving enzyme Hje cleaves only two strands, two nucleotides 3' of the junction centre. Hje is specific for strands that adopt a continous conformation in the stacked form of the junction
-
?
DNA + H2O
?
show the reaction diagram
-
catalytic centre: Asp70, Asp72 and Asp91
-
?
DNA + H2O
?
show the reaction diagram
-
cleaves the Holliday junction in a symmetrical mode by introducing two nicks in opposite strands across the junction. Cleavage of fixed cruciform DNA CFK1a11 and CFK1a01 which allows a branch migration over ten nucleotides. The pair of opposite strands are 01/0.3 and 02/04 in CFK1a01 and 11/13 and 12/14 in CFK1a11. CFK1a11 is cleaved at identical positions, three nucleotides 3' of the junction. Strong bias for cleavage axis 12/14 with more than 80% of the substrate being cleaved, while only less than 10% along axis 11713 is cleaved. CFK1a01 is cleaved along both axes with equal efficiency, cleavage positions
-
?
DNA + H2O
?
show the reaction diagram
Q9V0H1
cleaves the Holliday junction in a symmetrical mode by introducing two nicks in opposite strands across the junction. Cleavage of fixed cruciform DNA CFK1a11 and CFK1a01 which allows a branch migration over ten nucleotides. The pair of opposite strands are 01/0.3 and 02/04 in CFK1a01 and 11/13 and 12/14 in CFK1a11. CFK1a11 is cleaved at identical positions, three nucleotides 3' of the junction. Strong bias for cleavage axis 12/14 with more than 80% of the substrate being cleaved, while only less than 10% along axis 11713 is cleaved. CFK1a01 is cleaved along both axes with equal efficiency, cleavage positions
-
?
DNA + H2O
?
show the reaction diagram
-, Q9YEX2
cleaves the Holliday junction in a symmetrical mode by introducing two nicks in opposite strands across the junction. Cleavage of fixed cruciform DNA CFK1a11 and CFK1a01 which allows a branch migration over ten nucleotides. The pair of opposite strands are 01/0.3 and 02/04 in CFK1a01 and 11/13 and 12/14 in CFK1a11. CFK1a11 is cleaved at identical positions, three nucleotides 3' of the junction. Strong bias for cleavage axis 12/14 with more than 80% of the substrate being cleaved, while only less than 10% along axis 11713 is cleaved. CFK1a01 is cleaved along both axes with equal efficiency, cleavage positions
-
?
DNA + H2O
?
show the reaction diagram
-
cleaves the Holliday junction in a symmetrical mode by introducing two nicks in opposite strands across the junction. Cleavage of fixed cruciform DNA CFK1a11 and CFK1a01 which allows a branch migration over ten nucleotides. The pair of opposite strands are 01/0.3 and 02/04 in CFK1a01 and 11/13 and 12/14 in CFK1a11. CFK1a11 is cleaved at identical positions, three nucleotides 3' of the junction. Strong bias for cleavage axis 12/14 with more than 80% of the substrate being cleaved, while only less than 10% along axis 11713 is cleaved. CFK1a01 is cleaved more efficiently along the 01/04 axis, cleavage positions
-
?
DNA + H2O
?
show the reaction diagram
-
cleaves the Holliday junction in a symmetrical mode by introducing two nicks in opposite strands across the junction. Cleavage of fixed cruciform DNA CFK1a11 and CFK1a01 which allows a branch migration over ten nucleotides. The pair of opposite strands are 01/0.3 and 02/04 in CFK1a01 and 11/13 and 12/14 in CFK1a11. CFK1a11 is cleaved at identical positions, three nucleotides 3' of the junction. Strong bias for cleavage axis 12/14 with more than 80% of the substrate being cleaved, while only less than 10% along axis 11713 is cleaved. For the substrate CFK1a01 the enzyme has a strong bias for the 01/03 axis, cleavage positions
-
?
DNA + H2O
?
show the reaction diagram
P13340
cruciform DNA substrate CF110. High affinity for the Holliday structure containing one nick
-
?
DNA + H2O
?
show the reaction diagram
-
Holliday junction cleavage using 4Jh and Z28
-
?
DNA + H2O
?
show the reaction diagram
-
resolves the synthetic four-way junction X12
-
?
DNA + H2O
?
show the reaction diagram
-
the enzyme efficiently cleaves four-way junctions and less efficiently three-way junctions. The cleaved strand is rejoined by ligation, which means that cleavage occurs at the symmetrically related sites of the two strands, to leave 5'-phosphate and 3'-hydroxyl termini
-
?
DNA + H2O
?
show the reaction diagram
-
holliday structure
-
-
?
DNA + H2O
?
show the reaction diagram
-
holliday structure
-
-
?
DNA + H2O
?
show the reaction diagram
-
holliday structure
-
-
?
DNA + H2O
?
show the reaction diagram
-
holliday structure
-
-
?
DNA + H2O
?
show the reaction diagram
-
holliday structure
-
-
?
DNA + H2O
?
show the reaction diagram
-
the enzyme is required for mtDNA transmission and affects mtDNA content
-
?
DNA + H2O
?
show the reaction diagram
-
branched structure
-
-
?
DNA + H2O
?
show the reaction diagram
-
cleavage of Holliday junctions, different DNA substrates, 4-strand, 3-strand, Y-junction, flayed structure, 50-bp, 50-nt, 194-bp and 194-nt, annealing of ssDNA
-
-
?
DNA + H2O
?
show the reaction diagram
-
flap DNA
-
-
?
DNA + H2O
?
show the reaction diagram
-
Holliday structure HJ Jun3, Holliday structure HJ X12
-
-
?
DNA + H2O
?
show the reaction diagram
-
Holliday structure HJ-1
-
-
?
DNA + H2O
?
show the reaction diagram
-
Holliday structure HJbm4
-
-
?
DNA + H2O
?
show the reaction diagram
-
Holliday structure, junction Jbm5, catalytic site of Hje close to the N-terminus of strand betaB and a bend in betaC
-
-
?
DNA + H2O
?
show the reaction diagram
-
Holliday structure, RAD51C involved in HJ processing, catalysis of HJ resolution and ATP-dependent branch migration
-
-
?
DNA + H2O
?
show the reaction diagram
P39792
Holliday structure, RecU acts by making two simultaneous cuts in the phosphodiester backbone via its two active sites
-
-
?
DNA + H2O
?
show the reaction diagram
-
Holliday structure, RecU stimulates RecA binding to ssDNA and RecA-catalyzed D-loop formation but inhibits RecA-mediated three-strand exchange reaction and ssDNA-dependent dATP or rATP hydrolysis
-
-
?
DNA + H2O
?
show the reaction diagram
-
intriguing substrate preference for nicked Holliday junctions and D-loops, generating crossovers
-
-
?
DNA + H2O
?
show the reaction diagram
-
Rap mediates symmetrical resolution of 50bp and chi Holliday structures containing larger homologous cores
-
-
?
DNA + H2O
?
show the reaction diagram
Bacillus subtilis YB886
-
Holliday structure, RecU stimulates RecA binding to ssDNA and RecA-catalyzed D-loop formation but inhibits RecA-mediated three-strand exchange reaction and ssDNA-dependent dATP or rATP hydrolysis
-
-
?
DNA + H2O
?
show the reaction diagram
Q97YX6, -
a fixed junction with heterologous arms and a defined point of strand exchange. Holliday junction resolving enzyme Hjccleaves all four strands of the junction, three nucleotides 3' of the point of the strand exchange. Holliday junction resolving enzyme Hje cleaves only two strands, two nucleotides 3' of the junction centre. Hje is specific for strands that adopt a continous conformation in the stacked form of the junction
-
?
DNA + H2O
?
show the reaction diagram
Bacillus subtilis BG633
-
holliday structure
-
-
?
DNA junction 1 + H2O
?
show the reaction diagram
-
DNA junction 1 substrate assembled from strands b50, h50,r50,x50, r55, b1-27, b28-50
-
-
?
Holliday junction in DNA + H2O
?
show the reaction diagram
-
-
-
-
?
Holliday junction in DNA + H2O
?
show the reaction diagram
-
-
-
-
?
Holliday junction in DNA + H2O
?
show the reaction diagram
-
-
-
-
?
Holliday junction in DNA + H2O
?
show the reaction diagram
-
both recombinant AtMUS81-EME1A and AtMUS81-EME1B complexes can cleave the intact Holliday junction, however, the nicked form serves as a better substrate for both of the homologous complexes and was cut with higher efficiency than the intact form
-
-
?
Holliday junction in DNA + H2O
?
show the reaction diagram
-
GEN1 resolves Holliday junctions by the introduction of symmetrically related cuts across the junction point, to produce nicked duplex products in which the nicks can be readily ligated, GEN1 leaves ligatable nicks after symmetrical cleavage
-
-
?
Holliday junction in DNA + H2O
?
show the reaction diagram
-
RuvA protein binds Holliday junctions in preference to any other substrate
-
-
?
Holliday junction in DNA + H2O
?
show the reaction diagram
-
Yen1 resolves Holliday junctions by the introduction of symmetrically related cuts across the junction point, to produce nicked duplex products in which the nicks can be readily ligated, Yen1 leaves ligatable nicks after symmetrical cleavage
-
-
?
Holliday junction in DNA + H2O
?
show the reaction diagram
Q9UWX8
Sulfolobus has two distinct junction resolving enzymes, Hjc and Hje, with differing substrate specificities. The Hje and Hjc activities display pronounced differences in their patterns of cleavage of the junction, and no nucleotide positions are cleaved by both enzymes. Whilst Hje introduces multiple nicks in each arm of the mobile junction Jbm5, Hjc cuts each arm at only a single site. Hje introduces paired nicks on only the continuous h and x strands of the fixed junction J3, two nucleotides 3' of the point of strand exchange. In contrast, recombinant Hjc cleaves all four strands of the junction, with cleavage three nucleotides 3' of the junction centre
-
-
?
Holliday junction X0 + H2O
?
show the reaction diagram
-
GEN1 cuts the immobile junction X0 at a unique site located one nucleotide to the 3' side of the junction point
-
-
?
Holliday junction X0 + H2O
?
show the reaction diagram
-
Yen1 cuts the immobile junction X0 at a unique site located one nucleotide to the 3' side of the junction point
-
-
?
nXO12 junction in single-stranded DNA + H2O
?
show the reaction diagram
-
-
-
-
?
pXO12-3' junction in single-stranded DNA + H2O
?
show the reaction diagram
-
-
-
-
?
replication fork-like junction in DNA + H2O
?
show the reaction diagram
-
-
-
-
?
splayed Y junction in DNA + H2O
?
show the reaction diagram
-
-
-
-
?
Holliday junctions in DNA + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
class I substrates reflect low Km and high kcat and include the nicked Holliday junction, 3'-flapped and replication fork-like structures, class II substrates share low Km but low kcat relative to class I substrates and include the D-loop and partial Holliday junction, class III substrates are defined by splayed Y junctions having high Km and low Kcat
-
-
-
additional information
?
-
-
X12, nX12, 3'flap - EcME is able to convert all three substrates to linear duplex product
-
-
-
additional information
?
-
-
RuvA also stimulates RuvB helicase activity
-
-
-
additional information
?
-
-
RecU interacts with RecA and inhibits its single-stranded DNA-dependent dATP hydrolysis
-
-
-
additional information
?
-
-
ResT can use asymmetrized substrates that mimic the properties of a recombination site for a tyrosine recombinase, to form Holliday junctions
-
-
-
additional information
?
-
-
TRF2 contributes to t-loop stabilisation by stimulating Holliday junction formation and by preventing resolvase cleavage,TRF2 greatly increases the rate of Holliday junction formation and blocks the cleavage by various types of Holliday junction resolving activities, including the human GEN1 protein, the Myb-like domain of TRF2 slows the rate of junction migration, while the basic domain accelerates it
-
-
-
additional information
?
-
-
RusA cleaves Holliday junctions with high specificity and efficiency, and has comparatively little activity on other forms of branched DNAs unless these can adopt a four-way branched configuration mimicking a Holliday junction
-
-
-
additional information
?
-
-
cleavage of a four-way DNA junction by the human SLX1-SLX4 complex, overview
-
-
-
additional information
?
-
-
endonuclease I catalyses the breakage of the P-O3' bond
-
-
-
additional information
?
-
-
enzyme substrate specificity, overview. A specific interaction occurs between SIRV2 Holliday junction resolving enzyme, Hjr, and the SIRV2 virion body coat protein, SIRV2gp26
-
-
-
additional information
?
-
-
RecU binds in a nonspecific fashion to Holliday junction substrates and, in the presence of Mn2+, cleaves these substrates at a specific sequence 5'-G/TC2C/TTA/GG-3'. Amino acid residues E11, K31, D57, Y58, Y66, D68, E70, K72, T74, K76, Q88, and L92 may play either a direct or indirect role in the catalysis of Holliday junction resolution
-
-
-
additional information
?
-
-
RecU has two activities: in concert with RuvAB, it catalyzes the resolution of Holliday junctions, and, alone, it modulates RecA activities. RecU does not modulate RecA when it is bound to the Holliday junction
-
-
-
additional information
?
-
Q49422
RecUMge binds Holliday junction substrates and large double-stranded DNA molecules and cleaves Holliday junction substrates at the sequence 5'-G/TC-/-C/TTA/GG-3' in the presence of Mn2+, cleavage site determination, overview. RecUMge does not bind to small, linear dsDNA substrates. RecUMge cleavage of alternatively branched substrates, overview
-
-
-
additional information
?
-
-
substrate specificity of GEN1, and GEN1-Holliday junction complex structures, overview
-
-
-
additional information
?
-
-
activity with different constructs of Y-DNA under various packaging conditions, T4 endo VII resolvase cleavage sites in Y-DNAs, overview
-
-
-
additional information
?
-
-
oriented cleavage on Holliday junction 1 by FPV resolvase. Active site residues are D7, E60, K102, D132, and D135. For the wild-type complex in the presence of EDTA or Ca2+, migration is consistent with the DNA arms arranged in near-tetrahedral geometry. However, the D7N active-site mutant resolvase holds the arms in a more planar arrangement in EDTA, Ca2+, or Mg2+ conditions, implicating metal-dependent contacts at the active site in the larger architecture of the complex
-
-
-
additional information
?
-
-
usage of two plasmids containing hairpin four-way junctions constructed to assay resolving enzyme activity
-
-
-
additional information
?
-
-
RecU binds in a nonspecific fashion to Holliday junction substrates and, in the presence of Mn2+, cleaves these substrates at a specific sequence 5'-G/TC2C/TTA/GG-3'. Amino acid residues E11, K31, D57, Y58, Y66, D68, E70, K72, T74, K76, Q88, and L92 may play either a direct or indirect role in the catalysis of Holliday junction resolution
-
-
-
additional information
?
-
Q49422
RecUMge binds Holliday junction substrates and large double-stranded DNA molecules and cleaves Holliday junction substrates at the sequence 5'-G/TC-/-C/TTA/GG-3' in the presence of Mn2+, cleavage site determination, overview. RecUMge does not bind to small, linear dsDNA substrates. RecUMge cleavage of alternatively branched substrates, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
holliday structure
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
the enzyme is required for meiotic crossing over but not for gene conversion
-
?
DNA + H2O
hydrolyzed DNA
show the reaction diagram
-
the enzyme prevents mitochondrial DNA aggregation in Schizosaccharomyces pombe
-
?
DNA + H2O
?
show the reaction diagram
-
holliday structure
-
-
?
DNA + H2O
?
show the reaction diagram
-
the enzyme is required for mtDNA transmission and affects mtDNA content
-
?
DNA + H2O
?
show the reaction diagram
Bacillus subtilis BG633
-
holliday structure
-
-
?
additional information
?
-
-
RuvA also stimulates RuvB helicase activity
-
-
-
additional information
?
-
-
RusA cleaves Holliday junctions with high specificity and efficiency, and has comparatively little activity on other forms of branched DNAs unless these can adopt a four-way branched configuration mimicking a Holliday junction
-
-
-
additional information
?
-
-
cleavage of a four-way DNA junction by the human SLX1-SLX4 complex, overview
-
-
-
additional information
?
-
-
endonuclease I catalyses the breakage of the P-O3' bond
-
-
-
additional information
?
-
-
enzyme substrate specificity, overview. A specific interaction occurs between SIRV2 Holliday junction resolving enzyme, Hjr, and the SIRV2 virion body coat protein, SIRV2gp26
-
-
-
additional information
?
-
-
RecU binds in a nonspecific fashion to Holliday junction substrates and, in the presence of Mn2+, cleaves these substrates at a specific sequence 5'-G/TC2C/TTA/GG-3'. Amino acid residues E11, K31, D57, Y58, Y66, D68, E70, K72, T74, K76, Q88, and L92 may play either a direct or indirect role in the catalysis of Holliday junction resolution
-
-
-
additional information
?
-
-
RecU has two activities: in concert with RuvAB, it catalyzes the resolution of Holliday junctions, and, alone, it modulates RecA activities. RecU does not modulate RecA when it is bound to the Holliday junction
-
-
-
additional information
?
-
Q49422
RecUMge binds Holliday junction substrates and large double-stranded DNA molecules and cleaves Holliday junction substrates at the sequence 5'-G/TC-/-C/TTA/GG-3' in the presence of Mn2+, cleavage site determination, overview. RecUMge does not bind to small, linear dsDNA substrates. RecUMge cleavage of alternatively branched substrates, overview
-
-
-
additional information
?
-
-
substrate specificity of GEN1, and GEN1-Holliday junction complex structures, overview
-
-
-
additional information
?
-
-
RecU binds in a nonspecific fashion to Holliday junction substrates and, in the presence of Mn2+, cleaves these substrates at a specific sequence 5'-G/TC2C/TTA/GG-3'. Amino acid residues E11, K31, D57, Y58, Y66, D68, E70, K72, T74, K76, Q88, and L92 may play either a direct or indirect role in the catalysis of Holliday junction resolution
-
-
-
additional information
?
-
Q49422
RecUMge binds Holliday junction substrates and large double-stranded DNA molecules and cleaves Holliday junction substrates at the sequence 5'-G/TC-/-C/TTA/GG-3' in the presence of Mn2+, cleavage site determination, overview. RecUMge does not bind to small, linear dsDNA substrates. RecUMge cleavage of alternatively branched substrates, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
cannot replace Mg2+ or Mn2+ at concentrations between 1-500 mM
Ca2+
-
cannot replace Mn2+
Ca2+
-
Endo X3, 70% of the maximal activity obtained when Mg2+ is replaced by Ca2+
Ca2+
-
poor substitute for Mg2+
Ca2+
-
binding of two tetramers of RuvA on the junction is favored by divalent cations, Ca2+ enhances the binding of RuvA to the junction
Co2+
-
Endo X3 shows less than 10% of full activity at a concentration of 10 mM Co2+
Co2+
-
at 25 mM moderately effective for activity
Co2+
-
minor junction cleavage
Divalent cations
-
promote dissociation of SpCCE1
Divalent cations
-
required for activation
KCl
-
optimal concentration in reaction buffer: 200 mM
Mg2+
-
promotes dissociation of SpCCE1 by enabling strand cleavage
Mg2+
-
reduces binding of Rus A to the junction
Mg2+
-
optimum: 5-10 mM MgCl2
Mg2+
-
optimum: 15-30 mM MgCl2, 10% of maximal activity in 4 mM MgCl2
Mg2+
-
required for activation
Mg2+
-
Endo X3, optimum: 10 mM MgCl2, in presence of 10 mM MgCl2 the enzyme is salt sensitive
Mg2+
-
optimum: 8-25 mM, binding per se is independent of Mg2+, cleavage mechanism depends on Mg2+; required for activation
Mg2+
-
dependent on
Mg2+
-
optimal concentration: 10 mM
Mg2+
-
required for chi DNA cleavage, 0.1 mM is sufficient to promote stacking of the junction arms, at 1 mM no Rap-junction complexes were detected
Mg2+
-
initiation of reaction with 15 mM MgCl2 at 65C
Mg2+
-
10 mM optimal for resolution
Mg2+
-
modulates affinity of RecU for DNA, at low concetrations RecU binds to 3- and 4-strands with 12- and 46-fold higher affinity than to 194-nt or 194-bp DNA, and with > 50-fold higher affinity than to flayed, Y-junction, 50-nt and 50-bp DNA substrates, at high concentrations, RecU introduces specific cuts on mobile 4-strand substrates
Mg2+
-
the enzyme binds to stacked-X junctions in the presence of cations, in the absence of cations the enzyme binds to square-planar junctions
Mg2+
-
Asp88 and Glu101 essential for cation binding
Mg2+
-
BpuJI requires Mg2+-ions for DNA cleavage
Mg2+
-
a Mg2+ ion is present in each of the two active sites in the homodimeric enzyme
Mg2+
-
the endonuclease activity is optimal for the intact Holliday junction substrate at a range of 1 mM Mg2+ for both of the homologous complexes, a decrease in activity is observed at higher concentrations, Mg2+ can be replaced by Ca2+
Mg2+
-
the enzyme requires Mn2+ or Mg2+ as metal cofactors
Mg2+
-
required
Mg2+
Q9UWX8
strongly dependent on the presence of magnesium, with 15 mM Mg2+ ions optimal. Strong influence of magnesium ion concentrations on protein-junction complex stability. A dramatic shift in binding affinity is observed, with apparent dissociation constants for binding in the presence of 1.5, 2.5, 5 and 15 mM magnesium ions of 76 nM, 530 nM, 1100 nM and 1700 nM, respectively
MgCl2
-
required, optimal concentration: 5-10 mM
Mn2+
-
replacement of MgCl2 by equimolar amounts of MnCl2 results in a 50% loss of activity
Mn2+
-
Endo X3, 70% of the maximal activity obtained when Mg2+ is replaced by Mn2+
Mn2+
-
can substitute for Mg2+, but is required in higher amounts
Mn2+
-
required for chi DNA cleavage, reduced preference for cleavage in Mn2+ relative to Mg2+ on chi compared to small DNA substrates
Mn2+
-
supports activity as a cofactor to a higher extent then Mg2+ and leads to the formation of further cleavage products of lower molecular mass
Mn2+
-
preferred meta ion. The enzyme requires Mn2+ or Mg2+ as metal cofactors. Concentrations of Mn2+ above 3.3 mM inhibit cleavage
spermidine
-
-
Zn2+
-
cannot replace Mg2+ or Mn2+ at concentrations between 1-500 mM
Zn2+
-
cannot replace Mn2+
Zn2+
-
poor substitute for Mg2+
Zn2+
-
one atom per monomer
MnCl2
-
can substitute for MgCl2, less efficient
additional information
-
Ni2+ and Zn2+ cannot serve as cofactors for catalytic activity
additional information
-
influence of metal cofactors on the activity and structure of the resolvase of fowlpox virus, overview. No activity with Ca2+, little activity with Cu2+, Fe2+, Ni2+, and Zn2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
anti-Endo VII antibodies
-
Endo X3
-
Ca2+
-
strong inhibition
Cds1
-
the DNA replication checkpoint kinase Cds1 negatively regulates Mus81/Eme1 to preserve genomic integrity when replication is perturbed
-
EDTA
-
comple inhibition
KCl
-
reduces activity 10fold at a concentration of 200 mM
potassium glutamate
-
reduces activity 10fold at a concentration of 200 mM
RuvA
-
inhibits cleavage of certain DNA substrates
-
WRWYCR
-
inhibits junction cleavage
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
PCNA protein
-
Holliday junction-resolving enzyme Hjc interacts physically with PCNA via a canonical C-terminal PIP motif. This interaction stimulates the junction cleavage activity of Hjc in vitro. PCNA is a toroidal protein that acts as a processivity factor for many proteins. In Sulfolobus solfataricus, PCNA is a heterotrimer that can function as a molecular toolbelt, forming simultaneous interactions with up to three partner proteins with related functions in a DNA-processing pathway
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5.5e-06
-
3'-flapped junction in DNA
-
-
-
1.2e-06
-
D-loop junction in DNA
-
-
-
6.6e-05
-
DNA junction 1 substrate
-
at 15 mM MgCl2, 65C, pH 7
-
7.3e-05
-
DNA junction 1 substrate
-
at 5 mM MgCl2, 65C, pH 7
-
3.1e-06
-
nXO12 junction in single-stranded DNA
-
-
-
5.6e-06
-
pXO12-3' junction in single-stranded DNA
-
-
-
7.3e-06
-
replication fork-like junction in DNA
-
-
-
3.04e-05
-
splayed Y junction in DNA
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.12
-
3'-flapped junction in DNA
-
the 3'flap substrate contains 50 bp of duplex DNA, a central nick, and 25 bases of single-stranded DNA
-
0.97
-
3'-flapped junction in DNA
-
-
-
0.09
-
D-loop junction in DNA
-
-
-
0.0065
-
DNA junction 1
-
at 30C, steady-state approximation under maximal velocity conditions at 15 mM MgCl2
-
0.05
-
DNA junction 1
-
at 65C, pH 7, converting 6% of the substrate into product
-
0.00014
-
Holliday junction 3
-
at 50C
-
0.02
-
Holliday junction 3
-
prediction: at 80C
-
0.001
-
J1T1
-
-
-
0.00034
-
J1T2
-
-
-
6e-06
-
junction 1, unconstrained
-
E226N, 480fold reduced turnover rate
-
0.0029
-
junction 1, unconstrained
-
-
-
0.18
-
nX12 junction in single-stranded DNA
-
the nX12 substrate has four 25-bp duplex DNA arms, with a 12-bp homologous core that allows branch migration of the junction, and contains a nick at the cross-over point
-
1.2
-
nXO12 junction in single-stranded DNA
-
-
-
0.32
-
pXO12-3' junction in single-stranded DNA
-
-
-
0.00416
-
RC1
-
-
-
0.000566
-
RC1(1,3')
-
-
-
4.7e-06
-
RC1(2,3')
-
-
-
1.35
-
replication fork-like junction in DNA
-
-
-
0.26
-
splayed Y junction in DNA
-
-
-
0.0047
-
X12 junction in single-stranded DNA
-
like nX12, without the nick at the cross-over point
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
10
Q49422
broad optimum
7.5
-
Q9V301
assay at; assay at
7.5
-
Q97YX6, -
assay at
7.5
-
-
PCR fragment cleavage assay; plasmid and lambda DNA cleavage assay
7.5
-
-
nuclease assay
7.5
-
-
assay at
7.8
-
-
-
8
-
-
resolvase cleavage assay
8
-
-
endonuclease assay on pAT25; ligation assay
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
10
-
less than 50% of maximal activity above and below
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
PCR fragment cleavage assay; plasmid and lambda DNA cleavage assay
25
-
-
assay at
30
45
Q49422
broad optimum
30
-
-
steady-state approximation at 0.30 min-1 under maximal velocity conditions at 15 mM MgCl2
30
-
-
nuclease assay
37
-
-
-
37
-
-
resolvase cleavage assay
37
-
-
endonuclease assay on pAT25; ligation assay
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
60
-
Q9V301
assay at; assay at
60
-
Q97YX6, -
assay at
60
-
Q9UWX8
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
16
50
Q49422
activity range, inactive below or above
20
40
-
less than 50% of maximal activity above and below
45
65
-
no multiple turnover catalysis at lower temperatures measurable due to the sensitivity of the assay
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
PSNG13, Bloom's syndrome-associated, BLM, helicase-deficient fibroblasts, PSNF5, BLM-complemented fibroblasts
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
wild type enzyme and truncated enzyme forms DELTA1-35 and DELTA1-35/CDELTA15
-
Manually annotated by BRENDA team
additional information
-
in exponentially growing cells RecU is present throughout the cells, after addition of 100ng/mol MMC discrete focus in the nucleoid, in 2.7% of the cells two foci
-
Manually annotated by BRENDA team
additional information
Bacillus subtilis BG633
-
in exponentially growing cells RecU is present throughout the cells, after addition of 100ng/mol MMC discrete focus in the nucleoid, in 2.7% of the cells two foci
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
18000
-
-
Endo X3, SDS-PAGE
18600
-
-
calculation from amino acid sequence
22000
-
-
SDS-PAGE
23000
-
-
Endo X3, sedimentation in a sucrose density gradient
23950
-
-
MALDI-TOF MS
24000
-
-
SDS-PAGE
25000
-
-
gel-filtration
33000
-
-
gel filtration
38000
-
-
SDS-PAGE, enzyme has a globular shape
40000
-
-
gel filtration
40000
-
-
gel filtration
43000
-
-
Endo X3, gel filtration
53900
-
-
predicted molecular mass of the BpuJI subunit
73600
-
-
predicted molecular weight for His10-FLAG-Mus81, verified by PAGE
75500
-
-
MUS81 with N-terminal His-tag, gel filtration
82000
-
-
determined by gel filtration using a 3 microM EcME solution, heterodimer
106400
-
-
predicted molecular weight for GST-Mms4, verified by PAGE
109000
-
-
homodimer, determined by sedimentation equilibrium experiments using an analytical ultracentrifuge
140000
-
-
determined by gel filtration using a 88 microM EcME solution, heterotetramer
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Q9UWX8
x * 16010, calculated from sequence
dimer
-
2 * 30000, binds to the holliday junction as a dimer; exists as a monomer-dimer equilibrium in solution
dimer
-
homodimer
dimer
-
up to 2 dimers can bind to an X-junction
dimer
-
2 * 19000; homodimer
dimer
-
exists as a monomer-dimer equilibrium in solution
dimer
-
2 * 14300, wild-type enzyme, SDS-PAGE
dimer
-
crystallization, self-rotation function analysis
dimer
-
homodimer, 2 * 121930-135000, sedimentation and multi-angle light scattering
dimer
-
homodimer, 67000-158000, gel filtration, chemical cross linking, sedimentation and multi-angle light scattering
dimer
-
crystallographic 2fold rotation axis, Se-targeted SAD methods, dimeric in solution and in crystal
dimer
-
DTT reverses interactions between the enzyme and Holliday junction
dimer
-
determination of structure by MIR
dimer
P0AG74
-
heterodimer
-
Mus81-Eme1
heterodimer
-
one molecule of EcMus81 and one molecule of EcEme1
homodimer
-
-
homodimer
-
the endonuclease I forms an intimately associated symmetrical homodimer comprising two domains, each formed by residues 17-44 from one subunit and 50-145 from the other. The domains are connected by a bridge that forms part of an extended beta-sheet
octamer
-
active enzyme, in the presence of Mg2+, SDS-PAGE
tetramer
-
-
tetramer
-
SDS-PAGE
monomer
-
GEN1 protein contains the XPG-N, XPG-I, and helix-hairpin-helix domains essential for nuclease activity, linked to a C-terminal tail region that appears to be naturally disordered
additional information
-
Mus81 and Eme1 are subunits of nuclear Holliday junction resolvase
additional information
-
model of DNA bound in the active site of phage T7 endonuclease I
additional information
-
the RecU structure shows a mushroom-like appearance, with a cap and a stalk region. The RuvB interaction and the catalytic residues are located in the cap region of dimeric RecU, while the stalk region is essential not only for RecA modulation but also for Holliday junction recognition
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
cleavage activity of Mus81 is strictly regulated, part of this regulation occurs through post-translational modifications of Mus81
phosphoprotein
-
-
additional information
-
cleavage activity of Mus81 is strictly regulated, part of this regulation occurs through post-translational modifications of Mus81
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
prismatic crystals obtained by sparse-matrix screening and sitting-drop vapour-diffusion, plate-like crystals by counter-diffusion in X-ray capillary
-
at 17C, hanging drop method, in solution having a mushroom-like appearance, where the cap is formed by the main beta-sheet and flanking helices, structure of RecU superimposes best with PfHjc and archaeal HJR, the next best matches to RecU are a series of type II restriction endonucleases including EcoRV and Pvull
-
resolving the enzyme bound to DNA junctions, X-ray diffraction structure determination and analysis
-
hanging-drop method, 2.1 A resolution
-
the structures of RusA-D70N and RusA-D70N-DNA complex are determined at resolutions of 1.2 A and 3.1 A, respectively
P0AG74
three distinct crystal forms, form I: triclinic space group P1, resolution: 4 A, form II: not grown to a size sufficient for X-ray diffraction, form III: monoclinic space group P2-1, resolution: 2.5 A
-
improvements in crystallization conditions result in an increased resolution of the native enzyme crystal's diffraction data set of 1.4 A
-
the structure of Hjc is determined by using multiple-wavelength anomalous dispersion to a resolution of 2.15A
-
resolving enzymes bound to DNA junctions, X-ray diffraction structure determination and analysis
-
microbatch method with a silicone oil overlay, crystal structure at 2.0 A resolution
-
selenomethionine-containing enzyme crystallized by microbatch method with a silicone oil overlay, hexagonal form of the enzyme
-
sitting drop method, Mosquito nanolitre-drop crystallization robot, X-ray data collection
-
crystal structure of Sulfolobus Hjc, determined by using multiple-wavelength anomalous dispersion, to a resolution of 2.15 A
-
hanging-drop method at 20C
-
hanging-drop method, 2.4 A resolution
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
95
-
-
for 2 min followed by transfer on ice, inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the tetrameric RuvA-Holliday junction complex II is stable in the presence of 750 mM NaCl, whereas the same amount of salt induces more than 80% dissociation of the octameric complex I
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C, Tris-HCl buffer, 50% glycerol
-
-80C, Tris-HCl buffer, pH 8, 50% glycerol
-
-20C, stable for about 2 weeks
-
-20C, 0.6 ml enzyme solution were diluted with 0.6 ml glycerol
-
-20C, fraction VI of the Endo X3 purification can be stored after dialysis against buffer E
-
-20C, stable for at least 8 months without measurable loss of activity
-
on ice, fraction VI of the Endo X3 purification can be stored for over 1 month, should not be frozen
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gel filtration on Superose 12 column, > 98% purified
-
using heparin-Sepharose, blue-Sepharose and AH-Sepharose columns
-
99% purified, SDS-PAGE and Edman degradation
-
gel filtration on a Hi-Load (1.6 x 60 cm) Superdex 200 column, 90% purified by SDS-PAGE
-
phosphocellulose and DNA agarose chromatography, FPLC-gel filtration, 99% purified
-
amylose and heparin agarose chromatography of MBP-Rap, Rap29K, Rap-S and Rap17K
-
gel filtration of MBP-RuvC
-
highly purified
-
highly purified, 99% pure; RuvC
-
carboxy-terminal His-tagged GEN1 is purified using HisTrap column chromatography, heparin column chromatography, ssDNA column chromatography, and MonoS column chromatography
-
EcME is purified to apparent homogeneity through affinity chromatography, ion exchange, and gel filtration steps
-
purified to homogeneity
-
1873fold
-
DEAE-cellulose column chromatography, ammonium sulfate fractionation, Superdex-200 gel filtration, phosphocellulose column chromatography, and hydroxyapatite Bio-Gel HTP column chromatography
-
partial; partial
Q9V301
CCE1, 22fold to near homogeneity
-
Endo X3, more than 1325fold, purification beyond fraction V requires addition of pure protein like bovine serum albumin to a final concentration of 0.5 mg/ml
-
highly purified in bacteria, partially purified from the cognate host
-
overexpressed GST-Mms4/His10-Flag-Mus81 is purified by sequential affinity chromatography from Saccharomyces cerevisiae cells
-
produced in Escherichia coli
-
about 95% pure; YDC2
-
affinity-purified
-
purification of recombinant fusion protein MBP-YDC2
-
gel filtration, Superdex 75 column, greater than 98% purified
-
partial purification
-
partial; partial
Q97YX6, -
purified to homogeneity
-
affinity chromatography on amylose resin and gel filtration of MBP-A22
-
purified by dual affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
overexpression in Escherichia coli BL21
-, Q9YEX2
expressed in Escherichia coli
-
expression in Escherichia coli strain BL21(DE3) Codon Plus RIL
-
overexpression in Escherichia coli BL21
-
for expression in Escherichia coli ER2267 cells
-
expressed in Escherichia coli BL21(DE3)[pLysS] cells
-
expression in Escherichia coli BL21(DE3)(pLysS)
-
expression in Escherichia coli ruvABC-deficient strain
-
in Escherichia coli strain BL21(DE3)(pLysS) containing the recU overexpression plasmid pCB210
-
overexpression in Escherichia coli BL21(DE3)(pLysS) and XL1-Blue
-
gene gen-1, DNA and amino acid sequence determination and analysis. GEN-1 assignment and phylogenetic relationships
-
expression in Escherichia coli containing pMALc2
-
expression of covalently linked endonuclease VII dimers in Escherichia coli BL21
P13340
expressed in Escherichia coli
-
expression of MBP-RuvC in Escherichia coli strain ER2508
-
for expression in Escherichia coli
-
amino acids 260-551 for Mus81 and amino acids 244-571 for Eme1 are cloned for expression in Escherichia coli, the complex is named EcME
-
carboxy-terminal His-tagged GEN1 is expressed in Escherichia coli
-
for expression in Escherichia coli
-
overexpression in a baculovirus system
-
expression in Escherichia coli Bl21(DE3) strains Bl21-Al and Bl21 pLysS
-
expressed in Escherichia coli strain Origami (DE3)pLysS
-
gene MG352, expression of wild-type and mutant enzymes as MBP fusion protein sin Escherichia coli strain BL21(DE3)
-
gene RecUMge, DNA and amino acid sequence determination and analysis
Q49422
overexpression in Escherichia coli BL21
-, Q9V0H1
expression of mutant enzymes in Escherichia coli
-
overexpression in Escherichia coli BL21
-
cloning of MUS81 and MMS4 into GAL1/10 divergent promotor, 2 micro-based overexpression vector, based on pJN58
-
expressed in Saccharomyces cerevisiae strain W303
-
YEN1 coding sequence amplified from BY4741 genomic DNA and cloned into pDONR221. Further subcloning of the wild-type or mutant into pYES-DEST52 or pAG416GPD-ccdB-HA to generate pYES-DEST52-YEN1-V5-6xHis, pAG416GPD-YEN1-3xHA or pAG416GPDYEN1E193A/E195A-3xHA. Coding sequence of Yen1-V5-6xHis amplified from pYES-DEST52-YEN1-V5-6xHis and subcloned into the BamHI and HindIII sites of p416ADH to generate p416ADH-YEN1-V5-6xHis
-
construction of a MBP-YDC2 fusion protein
-
expression in Escherichia coli strain BL2 (DE3) Codon Plus RIL
-
cloning in Escherichia coli strain NEB 5 alpha, and expression in strain NEB Turbo and NEB T7 Express
-
expression in Escherichia coli
Q9UWX8
expression in Escherichia coli using vector pET19b-Hje with a native N-terminal
-
HJE gene cloned from genomic DNA into the pET19b Escherichia coli expression vector and the recombinant protein is expressed at high levels
-
cloned into the pDuetMxe vector for overexpression in Escherichia coli BL21DE3pLysS cells
-
expression of MBP-RuvC in Escherichia coli strain ER2508
-
expression of wild-type and mutant enzymes D30N and E81Q
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
F81A
-
naturally occuring mutant, that is sensitive to DNA-damaging agents as a null recU strain, a severely impaired enzyme. The mutant poorly recognizes and distorts Holliday junctions. At high concentrations, RecUF81A binds to Holliday junctions but fails to cleave them. RecUF81A does not inhibit RecA dATPase and strand-exchange activities and it loses structural selectivity for X-shaped structures. Phenotype, detailed overview
K56A
-
mutant with a putative separation-of-function phenotype, the mutant is about 5times less active than the wild type enzyme in cleavage of Holliday junctions, fails to inhibit the dATPase activity of RecA because it does not bind ssDNA
R71A
-
mutant with a putative separation-of-function phenotype, fails to inhibit the dATPase activity of RecA because it does not bind ssDNA
D292N
-
1.2fold decrease in binding of four-way DNA junction, 80fold decrease in catalytic activity
D293N
-
1.2fold decrease in binding of four-way DNA junction, more than 200fold decrease in catalytic activity
D294N
-
1.2fold decrease in binding of four-way DNA junction, more than 200fold decrease in catalytic activity
E145Q
-
0.85fold decrease in binding of four-way DNA junction, more than 200fold decrease in catalytic activity
E231A
-
21fold decrease in binding of four-way DNA junction, 4fold decrease in catalytic activity
F79A
-
70fold decrease in binding of four-way DNA junction, more than 200fold decrease in catalytic activity
K291A
-
130fold decrease in binding of four-way DNA junction, 47fold decrease in catalytic activity; 30fold decrease in binding of four-way DNA junction, more than 200fold decrease in catalytic activity
K291R
-
130fold decrease in binding of four-way DNA junction, more than 200fold decrease in catalytic activity
Q147A
-
7.5fold decrease in binding of four-way DNA junction, 100fold decrease in catalytic activity
R146A
-
70fold decrease in binding of four-way DNA junction, more than 200fold decrease in catalytic activity
R150A
-
18fold decrease in binding of four-way DNA junction, 70fold decrease in catalytic activity
R231K
-
330fold decrease in binding of four-way DNA junction, more than 200fold decrease in catalytic activity
D70N
P0AG74
catalytically inactive mutant
E68G/H136R
-
the mutation affects octamer formation, DNA binding, and the stimulation of RuvB helicase activity
H29R/E40G/E68G/K129E/F140S/S177G/D184N
-
the mutation affects octamer formation, DNA binding and the stimulation of RuvB helicase activity
H29R/E40G/Q58R/K129E/F140S/S177G/D184N
-
the mutation affects octamer formation, DNA binding and the stimulation of RuvB helicase activity
K76Q
-
failure of the mutant enzyme to promote DNA repair
N73A
-
mutant enzyme with 20% of the wild-type activity at 50 nM protein concentration
N79D/N100D
-
the mutation affects octamer formation, DNA binding and the stimulation of RuvB helicase activity
R69A
-
failure of the mutant enzyme to promote DNA repair
R69Q
-
failure of the mutant enzyme to promote DNA repair
D132A
-
site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme
D132C
-
site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme
D135A
-
site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme
D135C
-
site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme
D135N
-
site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme
D55A
-
site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme
D7A
-
site-directed mutagenesis, inactive mutant
D7C
-
site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme
D7N
-
site-directed mutagenesis, inactive mutant, the active-site mutant resolvase holds the arms in a more planar arrangement in EDTA, Ca2+, or Mg2+ conditions
E33A
-
site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme
E60A
-
site-directed mutagenesis, inactive mutant
E60C
-
site-directed mutagenesis, mutant with reduced activity, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme
E60N
-
site-directed mutagenesis, mutant with reduced activity, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme
E60Q
-
site-directed mutagenesis, inactive mutant
K102A
-
site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme
K102R
-
site-directed mutagenesis, mutant enzyme activity with Mg2+ or Mn2+ compared to the wild-type enzyme
R13M
-
mutant is used to include a second methionine in addition to Met-56
D307A
-
D307 is critical for catalysis
D338A/D339A
-
mutant, lacking potential catalytic residues
D8N
-
mutant defective in one of four conserved residues known to comprise the catalytic site, slightly improved binding to DNA but unable to cleave it
D112A
-
site-directed mutagenesis, the mutant shows unaltered Holliday junction binding and cleaving activities
D57A
-
site-directed mutagenesis, the mutant shows unaltered Holliday junction binding but no cleaving activities
D68A
-
site-directed mutagenesis, the mutant shows unaltered Holliday junction binding but no cleaving activities
E11A
-
site-directed mutagenesis, the mutant shows unaltered Holliday junction binding but no cleaving activities
E70A
-
site-directed mutagenesis, the mutant shows unaltered Holliday junction binding but no cleaving activities
F103A
-
site-directed mutagenesis, inactive mutant without Holliday junction binding or cleaving activities
F108A
-
site-directed mutagenesis, inactive mutant without Holliday junction binding or cleaving activities
F69A
-
site-directed mutagenesis, inactive mutant without Holliday junction binding or cleaving activities
F79A
-
site-directed mutagenesis, inactive mutant without Holliday junction binding or cleaving activities
G100A
-
site-directed mutagenesis, inactive mutant without Holliday junction binding or cleaving activities
G60A
-
site-directed mutagenesis, inactive mutant without Holliday junction binding or cleaving activities
G64A
-
site-directed mutagenesis, the mutant shows slightly reduced Holliday junction binding but unaltered cleaving activities compared to the wild-type enzyme
G7A
-
site-directed mutagenesis, the mutant shows unaltered Holliday junction binding but reduced cleaving activities compared to the wild-type enzyme
H87A
-
site-directed mutagenesis, the mutant shows unaltered Holliday junction binding but reduced cleaving activities compared to the wild-type enzyme
H91A
-
site-directed mutagenesis, inactive mutant without Holliday junction binding or cleaving activities
K31A
-
site-directed mutagenesis, the mutant shows reduced Holliday junction binding activity and no cleaving activity
K72A
-
site-directed mutagenesis, the mutant shows reduced Holliday junction binding activity and no cleaving activity
K76A
-
site-directed mutagenesis, the mutant shows reduced Holliday junction binding activity and no cleaving activity
L10A
-
site-directed mutagenesis, the mutant shows reduced Holliday junction binding and cleaving activities
L122A
-
site-directed mutagenesis, the mutant shows unaltered Holliday junction binding but reduced cleaving activities compared to the wild-type enzyme
L92A
-
site-directed mutagenesis, the mutant shows reduced Holliday junction binding activity and no cleaving activity
N15A
-
site-directed mutagenesis, the mutant shows slightly reduced Holliday junction binding and cleaving activities
N5A
-
site-directed mutagenesis, the mutant shows unaltered Holliday junction binding and cleaving activities
Q88A
-
site-directed mutagenesis, the mutant shows unaltered Holliday junction binding but no cleaving activities
S54A
-
site-directed mutagenesis, the mutant shows slightly reduced Holliday junction binding and cleaving activities
T74A
-
site-directed mutagenesis, the mutant shows reduced Holliday junction binding activity and no cleaving activity
V46A
-
site-directed mutagenesis, the mutant shows unaltered Holliday junction binding but reduced cleaving activities compared to the wild-type enzyme
Y58A
-
site-directed mutagenesis, the mutant shows reduced Holliday junction binding activity and no cleaving activity
Y62A
-
site-directed mutagenesis, the mutant shows slightly reduced Holliday junction binding but unaltered cleaving activities compared to the wild-type enzyme
Y66A
-
site-directed mutagenesis, the mutant shows reduced Holliday junction binding activity and no cleaving activity
G64A
-
site-directed mutagenesis, the mutant shows slightly reduced Holliday junction binding but unaltered cleaving activities compared to the wild-type enzyme
-
H91A
-
site-directed mutagenesis, inactive mutant without Holliday junction binding or cleaving activities
-
K72A
-
site-directed mutagenesis, the mutant shows reduced Holliday junction binding activity and no cleaving activity
-
D33A
-
no cleavage of Holliday junction
D33A
-
mutant enzyme retains proper binding ablity to the Holliday junction
DELTA1-5
-
mutation causes a considerable decrease in Hjc-Holliday junction complex formation and cleavage activity
E110A
-
mutant enzyme is as active as the wild-type enzyme
E11A
-
mutant enzyme is as active as the wild-type enzyme
E46A
-
no cleavage of Holliday junction
E9A
-
no cleavage of Holliday junction
F21A
-
mutant enzyme is as active as the wild-type enzyme
F68A
-
no cleavage of Holliday junction
F72A
-
no cleavage of Holliday junction. Mutant enzyme exists as monomer more frequently in solution than as dimer
F89A
-
mutant enzyme is as active as the wild-type enzyme
K30A/K31A
-
mutant enzyme retains proper binding ability to the Holliday junction, little or almost no cleavage activity
K48A
-
no cleavage of Holliday junction. Mutant enzyme exists as monomer more frequently in solution than as dimer
K51A/K52A
-
mutant enzyme retains proper binding ability to the Holliday junction, weak cleavage activity
K81A
-
no cleavage of Holliday junction
R10A
-
no cleavage of Holliday junction
R25A
-
no cleavage of Holliday junction
R3A/K4A
-
mutation reduces the activity by 20fold as compared with the wild-type enzyme. The binding to the Holliday junction is substantially lowered
Y56A
-
some decrease in activity
D414A/D415A
-
mutations introduce a diagnostic NheI restriction site
DELTA1-35
-
mutant enzyme is not able to resolve the synthetic four-way junction X12
DELTA1-35/CDELTA15
-
mutant enzyme is not able to resolve the synthetic four-way junction X12
T239A
-
mutant lacking Cds1-dependent regulation
S30A
-
serine 30 on a flexible loop is catalytically essential, mutants show a decrease in catalytic rate of 3-4 orders of magnitude
S30C
-
serine 30 on a flexible loop is catalytically essential, mutants show a decrease in catalytic rate of 3-4 orders of magnitude
S30T
-
has a slightly higher activity than mutants S30A and S30C but is still severely compromised
D151A
-
mutant with amino acid active site substitution
D151N
-
mutant with amino acid active site substitution
D152A
-
mutant with amino acid active site substitution
D152N
-
mutant with amino acid active site substitution
D155A
-
mutant with amino acid active site substitution
D30A
-
mutant with amino acid active site substitution
D30N
-
mutation eliminates catalytic activity without affecting specific DNA binding
D30N
-
mutant with amino acid active site substitution
D81Q
-
mutation eliminates catalytic activity without affecting specific DNA binding
E81A
-
mutant with amino acid active site substitution
E81Q
-
mutant with amino acid active site substitution
K124A
-
mutant with amino acid active site substitution
R121A
-
mutant with amino acid active site substitution
Y80A
-
naturally occuring mutant showing an an intermediate phenotype. The mutant poorly recognizes and distorts Holliday junctions, and cleaves them with low efficiency. RecUY80A does not inhibit RecA dATPase and strand-exchange activities and it loses structural selectivity for X-shaped structures. Phenotype, detailed overview
additional information
-
gen-1 mutants are defective in DNA damage-dependent cell cycle arrest and apoptosis and in positional cloning of GEN-1, phenotypes, detailed overview
K76R
-
failure of the mutant enzyme to promote DNA repair
additional information
-
RusA restores viability to polA, dam, and uvrD mutant cells lacking RuvABC
M8A
-
site-directed mutagenesis, the mutant shows unaltered Holliday junction binding and cleaving activities
additional information
-
generation of a series of 16 deletion mutants, 9 N- and 7 C-terminal deletion mutants, and 31 point mutants of RecUMge. Deletion of more than 8 amino acid residues renders the mutants inactive, overview
K76A
-
site-directed mutagenesis, the mutant shows reduced Holliday junction binding activity and no cleaving activity
-
additional information
-
generation of a series of 16 deletion mutants, 9 N- and 7 C-terminal deletion mutants, and 31 point mutants of RecUMge. Deletion of more than 8 amino acid residues renders the mutants inactive, overview
-
E193A/E195A
-
catalytically inactive
additional information
-
construction of mms4DELTA and yen1DELTA deletion mutants, and of the double mutant mms4DELTA/yen1DELTA showing high sensitivity to DNA damage and a specific reduction in crossover events. Genetic interactions of mms4DELTA and yen1DELTA, overview
E226N
-
inactive mutant of YDC2
additional information
-
cells that lack Holliday junction resolvase Ydc2 show a significant depletion of mtDNA content. Truncated mutants lacking the SAP motif alone or the whole triple-helix domain are not functional in yeast mitochondria
additional information
-
Spcce1:ura4+ insertion mutant strain devoid of the Holliday junction resolvase activity. The majority of mitochondrial DNA from the mutant strain is in an aggregated form apparently due to extensive interlinking of DNA molecules by recombinant junctions. This marked effect on the conformation of mitochondrial DNA results in little or no effect on proliferation or viability of the mutant strain
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
its deficiency may lead to genome instability and cancer
medicine
-
development of antiviral agents against poxviruses