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Information on EC 3.1.26.4 - ribonuclease H and Organism(s) Mus musculus and UniProt Accession Q9CWY8

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.26 Endoribonucleases producing 5'-phosphomonoesters
                3.1.26.4 ribonuclease H
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Mus musculus
UNIPROT: Q9CWY8 not found.
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The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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Endonucleolytic cleavage to a 5'-phosphomonoester
Synonyms
reverse transcriptase, ribonuclease h, rnase h2, rnase hii, rnaseh2a, rnaseh1, ribonuclease hi, ribonuclease h2, rnase hiii, ribonuclease h1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
endoribonuclease H
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hybrid nuclease
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hybrid ribonuclease
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hybridase
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hybridase (ribonuclease H)
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nuclease, hybrid ribo-
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nuclease, ribo-, H
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P32
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ribonuclease H
RNA*DNA hybrid ribonucleotidohydrolase
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RNase H
RNase H1
RNase HI
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RNase HII
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RNase HIII
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Rnaseh1
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Endonucleolytic cleavage to a 5'-phosphomonoester
show the reaction diagram
active site geometry suggests a two-metal ion-dependent catalytic mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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CAS REGISTRY NUMBER
COMMENTARY hide
9050-76-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
poly(rAdT) + H2O
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show the reaction diagram
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?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
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enzyme form H2 is mostly inactive at low salt and requires 100-200 mM concentration for maximal activity. KCl is more efficient than NaCl
Mn2+
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enzyme form H1: requirement for a divalent metal ion can be satisfied by Mg2+ or with a stronger preference with Mn2+
NaCl
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enzyme form H2 is mostly inactive at low salt and requires 100-200 mM concentration for maximal activity. KCl or NH4Cl is more efficient than NaCl
NH4Cl
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enzyme form H2 is mostly inactive at low salt and requires 100-200 mM concentration for maximal activity. NH4Cl is more efficient than NaCl
additional information
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RNases H act as dimers, with two Mg2+ or other divalent cations being essential for correct protein structure, stability and enzyme activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
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calcium ions generally inactivate the enzyme and abolish catalysis
Dextran
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EDTA
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Ethidium bromide
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KCl
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activity of enzyme form H1 decreases rapidly above 50 mM and becomes nearly abolished at 150 mM
NaCl
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activity of enzyme form H1 decreases rapidly above 50 mM and becomes nearly abolished at 150 mM
NEM
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enzyme form H2. No effect on enzyme form H1
NH4Cl
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activity of enzyme form H1 decreases rapidly above 50 mM and becomes nearly abolished at 150 mM
Nucleic acids
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enzyme form H1 is more susceptible to inhibition than enzyme form H2
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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enzyme form H2 is inactive in absence of mercaptoethanol. No effect on enzyme form H1
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0005
poly(rAdT)
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lower than 0.0005 mM
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additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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enzyme form H-2
8.4
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enzyme form H-1
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 8.4
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pH 6.8: about 60% of maximal activity, pH 8.4: about 35% of maximal activity, enzyme form H-2
7.5 - 9
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about 45% of maximal activity at pH 7.5 and at pH 9.0, enzyme form H-1
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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line MOPC-21
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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nuclear RNase H1
Manually annotated by BRENDA team
additional information
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translation initiates at each of the two in-frame AUGs of the Rnaseh1 mRNA, with the longer form being imported into mitochondria, subcellular localization study, overview
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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reverse transcriptase (RT) and ribonuclease H are among the most ancient and abundant protein folds. RNases H may have evolved from ribozymes, related to viroids, early in the RNA world, forming ribosomes, RNA replicases and polymerases. Basic RNA-binding peptides enhance ribozyme catalysis. RT and ribozymes or RNases H are present today in bacterial group II introns, the precedents of transposable elements. Thousands of unique RTs and RNases H are present in eukaryotes, bacteria, and viruses
malfunction
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mice deficient in RNase H1 that localizes to mitochondria die during embryogenesis, probably due to the defective processing of R-loops. RNase H2 knockout mice are also not viable, and mutations in either of the human genes can cause Aicardi-Goutieres Syndrome, a severe inheritable neurodevelopmental disorder. In this disease, uncleaved RNA-DNA hybrids accumulate within cells that possibly upregulate interferon via the nucleic acid sensor cyclic GMP-AMP synthase (cGAS) and its adaptor protein STING
physiological function
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the RNase H enzymes mediate viral and cellular replication and antiviral defense in eukaryotes and prokaryotes, splicing, R-loop resolvation, DNA repair. RNase H-like activities are also required for the activity of small regulatory RNAs. Virtually all known immune defense mechanisms against viruses, phages, transposable elements, and extracellular pathogens require RNase H-like enzymes. RNase H-like activities of retroviruses, transposable elements, and phages, have built up innate and adaptive immune systems throughout all domains of life. R-loops are formed when an RNA strand intercalates into dsDNA, resulting in RNA-DNA hybrids and single-stranded DNA loops. R-loops affect promoter activities, with a role in gene expression (e.g. of the c-Myc proto-oncogene), genome stability, CRISPR-Cas immunity, DNA repair, and cancer formation. RNases H can remove the RNA moiety and prevent deleterious DNA breaks
additional information
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translation initiates at each of the two in-frame AUGs of the Rnaseh1 mRNA, with the longer form being imported into mitochondria, regulation mechanisms, modelling, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RNH2A_MOUSE
301
0
33513
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
105000 - 110000
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enzyme form H1, gel filtration
30000
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x * 30000, about, mitochondrial RNase H1, SDS-PAGE
33000
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x * 33000, enzyme form H2, SDS-PAGE
36000 - 40000
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enzyme form H2, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
heterotrimeric complex of the RNase H2A, RNase H2B, and RNase H2C proteins, crystallization data
dimer
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RNases H act as dimers, with two Mg2+ or other divalent cations being essential for correct protein structure, stability and enzyme activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
heterotrimeric complex of the RNase H2A, RNase H2B, and RNase H2C proteins, to 3.1 A resolution. The overall structure reveals an elongated arrangement of the subunits with the H2C protein in the middle flanked by the H2A and H2B proteins on the ends. Construction of a model for an Okazaki fragment binding to the mouse RNase H2 complex. In the model, the double-stranded RNA-DNA molecule runs through the active site cleft and is positioned to make several favorable electrostatic interactions and no significant steric clashes with the protein. The RNA-DNA hybrid is situated so that the target phosphodiester bond is in the proper orientation for nucleophile attack initiated by a two-metal ion chemistry
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D142N
mutation in strictly positionally conserved acidic residues, complete loss of activity
D170N
mutation in strictly positionally conserved acidic residues, complete loss of activity
D34N
mutation in strictly positionally conserved acidic residues, complete loss of activity
E35A
mutation in strictly positionally conserved acidic residues, complete loss of activity
G37S
mutation in subunit H2A identified in patients with Aicardi-Goutieres' syndrome. Mutation appears to distort the active site accounting for the demonstrated substrate specificity modification
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme form H-1 and H-2
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partial, two types of enzyme: H1 and H2
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene rnaseh1, translation initiates at each of the two in-frame AUGs of the Rnaseh1 mRNA, with the longer form being imported into mitochondria, regulation mechanisms, overview. Recombinant enzyme expression in Flp-In T-Rex-293 cells, and in vitro translation.
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Crouch, R.J.; Dirksen, M.L.
Ribonuclease H
Cold Spring Harbor Monogr. Ser.
14
211-254
1982
Bos taurus, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Mus musculus, Rattus norvegicus, Xenopus laevis
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Manually annotated by BRENDA team
O'Cuinn, G.; Persico, F.J.; Gottlieb, A.A.
Two ribonuclease H activities from the murine myeloma, MOPC-21
Biochim. Biophys. Acta
324
78-85
1973
Mus musculus
Manually annotated by BRENDA team
Cathala, G.; Rech, J.; Huet, J.; Jeanteur, P.
Isolation and characterization of two types of ribonucleases H in Krebs II ascites cells
J. Biol. Chem.
254
7353-7361
1979
Mus musculus
Manually annotated by BRENDA team
Shaban, N.M.; Harvey, S.; Perrino, F.W.; Hollis, T.
The structure of the mammalian RNase H2 complex provides insight into RNA.NA hybrid processing to prevent immune dysfunction
J. Biol. Chem.
285
3617-3624
2010
Mus musculus (Q9CWY8), Mus musculus
Manually annotated by BRENDA team
Suzuki, Y.; Holmes, J.B.; Cerritelli, S.M.; Sakhuja, K.; Minczuk, M.; Holt, I.J.; Crouch, R.J.
An upstream open reading frame and the context of the two AUG codons affect the abundance of mitochondrial and nuclear RNase H1
Mol. Cell. Biol.
30
5123-5134
2010
Mus musculus
Manually annotated by BRENDA team
Moelling, K.; Broecker, F.; Russo, G.; Sunagawa, S.
RNase H as gene modifier, driver of evolution and antiviral defense
Front. Microbiol.
8
1745
2017
Saccharomyces cerevisiae, Homo sapiens, Mus musculus, Escherichia coli (P0A7Y4)
Manually annotated by BRENDA team