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Information on EC 3.4.21.B30 - UmuD protein and Organism(s) Escherichia coli and UniProt Accession P0AG11
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3.4.21.B30 UmuD proteinSpecify your search results
Word Map
- 3.4.21.B30
- reca
-
translesion
-
mucab
- polymerases
-
damage-induced
-
uv-induced
-
reca-mediated
-
mutable
-
mutability
-
umud\'c
-
transversions
-
error-free
-
sos-induced
-
abasic
-
sos-regulated
-
self-cleavage
-
replication-blocking
-
n-2-acetylaminofluorene
-
reca430
-
sos-independent
-
y-family
-
at->ta
-
lexadef
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
involved in UV protection and mutation. Essential for induced (or SOS) mutagenesis. May modify the DNA replication machinery to allow bypass synthesis across a damaged template
Synonyms
umudc, umud', dna damage response protein, umudab, umud protein, umud2, umudpr, polymerase manager protein umud, umudpr protein, error-prone polymerase accessory, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
UmuD'
UmuD'
-
UmuD is initially produced as a 139-amino-acid protein, which subsequently cleaves off its N-terminal 24 amino acids in a reaction dependent on RecA/single-stranded DNA, giving UmuD'
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
CAS REGISTRY NUMBER
COMMENTARY
98059-81-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UmuD + H2O
?
UmuD undergoes cleavage upon interaction with a RecA/ssDNA complex
-
-
?
UmuD2 + H2O
UmuD2' + ?
-
autocleavage removes the N-terminal 24 amino acids of each UmuD2 to the remaining fragment UmuD2'
-
-
?
UmuD2 + H2O
UmuD2' + ?
-
slow auto-cleavage of UmuD2 to UmuD'2. The wild-type UmuD homodimer cleaves in both cis and trans conformations
-
-
?
additional information
?
-
-
binds to a cleft located between two RecA monomers in the crystal structure
-
?
additional information
?
-
-
interacts with RecA-DNA filament and participates in mutagenesis
-
?
additional information
?
-
-
UmuD and UmuD' interact differently with polymerase III: whereas uncleaved UmuD interacts more strongly with beta than it does with alpha, UmuD' interacts more strongly with alpha than with beta
-
?
additional information
?
-
-
UmuD' protein is a component of DNA polymerase V
-
?
additional information
?
-
-
UmuD' protein is a component of DNA polymerase V, role in translesion DNA synthesis
-
?
additional information
?
-
-
the damage-induced RecA:ssDNA nucleoprotein filament facilitates autocleavage of the N-terminal 24-amino acids of UmuD2 to yield UmuD'2, the form that enables mutagenesis
-
-
?
additional information
?
-
-
UmuD2 undergoes autodigestion at elevated pH
-
-
?
additional information
?
-
-
enzyme UmuD does not bind DNA. the enzyme UmuD interacts with several components of DNA polymerase III, including the polymerase subunit alpha, the beta clamp and the proofreading subunit epsilon, homology modeling and protein-protein docking analysis, overview. It interacts with the alpha subunit of DNA polymerase III at two distinct binding sites, one of which is adjacent to the single-stranded DNA-binding site. Enzyme UmuD specifically inhibits binding of DNA polymerase III alpha to ssDNA, UmuD residues D91 and G92 are involved in this interaction, molecular modeling, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
binds to a cleft located between two RecA monomers in the crystal structure
-
?
additional information
?
-
-
interacts with RecA-DNA filament and participates in mutagenesis
-
?
additional information
?
-
-
UmuD and UmuD' interact differently with polymerase III: whereas uncleaved UmuD interacts more strongly with beta than it does with alpha, UmuD' interacts more strongly with alpha than with beta
-
?
additional information
?
-
-
UmuD' protein is a component of DNA polymerase V
-
?
additional information
?
-
-
UmuD' protein is a component of DNA polymerase V, role in translesion DNA synthesis
-
?
additional information
?
-
-
the damage-induced RecA:ssDNA nucleoprotein filament facilitates autocleavage of the N-terminal 24-amino acids of UmuD2 to yield UmuD'2, the form that enables mutagenesis
-
-
?
additional information
?
-
-
UmuD2 undergoes autodigestion at elevated pH
-
-
?
additional information
?
-
-
enzyme UmuD does not bind DNA. the enzyme UmuD interacts with several components of DNA polymerase III, including the polymerase subunit alpha, the beta clamp and the proofreading subunit epsilon, homology modeling and protein-protein docking analysis, overview. It interacts with the alpha subunit of DNA polymerase III at two distinct binding sites, one of which is adjacent to the single-stranded DNA-binding site. Enzyme UmuD specifically inhibits binding of DNA polymerase III alpha to ssDNA, UmuD residues D91 and G92 are involved in this interaction, molecular modeling, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DNA polymerase III
-
UmuD interacts with the beta subunit of DNA polymerase III
-
RecA
-
MucA undergoes RecA-mediated cleavage and autocatalysis at alkaline pH
-
RecA
-
UmuD undergoes RecA-mediated cleavage and autocatalysis at alkaline pH, the larger product UmuD' is active and required for damge-induced mutagenesis
-
RecA
-
required for activity, RecA facilitates the intermolecular selfcleavage of UmuD2 homodimer
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
malfunction
metabolism
-
competition between enzyme UmuD and ssDNA for DNA polymerase III alpha binding is a distinct mechanism for polymerase exchange
physiological function
additional information
physiological function
UmuD regulates the cellular response to DNA damage
physiological function
the umuD gene products are upregulated after DNA damage and play roles in both nonmutagenic and mutagenic aspects of the SOS response
malfunction
-
effects of recA and umuD mutations on UmuDAb cleavage in DNA damage response of Escherichia coli
malfunction
-
for cleavage to occur, UmuD S60A and UmuD G25D mutant dimers must first exchange in the presence of RecA:ssDNA, and any cleavage detected results from cleavage in trans. Cleavage is less efficient in this context, indicating that the decreased rate of cleavage in the trans dimers results from the time required for dimer exchange to first take place before cleavage can occur
physiological function
-
the active form of DNA polymerase V is UmuD'2C-RecA-ATP. RecA* transfers a single RecA-ATP stoichiometrically from its DNA 3'-end to free pol V (UmuD'2C) to form an active mutasome with the composition UmuD'2C-RecA-ATP
physiological function
-
UmuD is implicated in a primitive DNA damage checkpoint and prevents DNA polymerase IV-dependent -1 frameshift mutagenesis, while the cleaved form UmuD' facilitates UmuC-dependent mutagenesis via formation of DNA polymerase V (UmuD'2C). Thus, the cleavage of UmuD is a crucial switch that regulates replication and mutagenesis via numerous protein-protein interactions.
physiological function
-
UmuD2, when bound to DinB, displaces the equilibrium in favor of the non-slipped conformation, thereby preventing frameshifting and potentially enhancing DinB activity on non-slipped substrates. DinB template slippage is inhibited by UmuD2
physiological function
-
UmuD is a dynamic protein that regulates mutagenesis. The UmuD gene products, regulated by the SOS response, exist in two principal forms: UmuD2, which prevents mutagenesis, and UmuD2, which facilitates UV-induced mutagenesis. UmuD slows the resumption of DNA replication after UV irradiation. UmuD interacts with DinB and inhibits its mutagenic -1 frameshift activity. UmuD2 interacts with the RecA/ssDNA filament, which stimulates the ability of UmuD to cleave itself
physiological function
-
UmuD2 is the initial umuD gene product that appears after induction of the SOS response. It is involved in regulating mutagenesis as part of the tightly controlled SOS response
physiological function
-
the protein UmuD is extensively involved in modulating cellular responses to DNA damage and may play a role in DNA polymerase exchange for damage tolerance. The polymerase manager protein UmuD directly regulates Escherichia coli DNA polymerase III alpha binding to ssDNA
physiological function
-
The umuD gene products perform distinct functions in preventing and facilitating mutagenesis. The full-length dimeric UmuD2 is the initial product that is expressed shortly after the induction of the SOS response and inhibits bacterial mutagenesis, allowing for error-free repair to occur. The slow auto-cleavage of UmuD2 to UmuD'2 promotes mutagenesis to ensure cell survival. The intracellular levels of UmuD2 and UmuD?2 are further regulated by degradation in vivo, returning the cell to a nonmutagenic state. Dynamic regulatory roles of the umuD gene, overview. UmuD lifecycle involves dimer exchange and cleavage in the regulation of the DNA damage respons
physiological function
-
when bound to UmuC, the enzyme functions as a checkpoint in delaying cell division, allowing time for error-free repair mechanisms to act, error-prone polymerase accessory UmuD. UmuD is not required for UmuDAb expression from its native promoter, nor its disappearance after DNA damage through intermolecular interactions with Escherichia coli UmuD
additional information
-
intermolecular mechanism of UmuD self-cleavage of enzyme dimers, overview
additional information
-
UmuD proteins are shown to adopt multiple conformations in solution, homology models of UmuD and the structure of UmuD', overview. The heterodimer is the predominant UmuD protein conformer
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
UmuD and the cleavage product UmuD' exist as homodimers. Their subunits can readily exchange to form UmuDD' heterodimers preferentially. Heterodimer formation is an essential step in the degradation pathway of UmuD'
dimer
homodimer
additional information
dimer
-
although UmuD and UmuD' form homodimers, they preferentially form heterodimers, crosslinking experiments, SDS-PAGE
dimer
-
although UmuD and UmuD' form homodimers, they preferentially form heterodimers, SDS-PAGE
dimer
-
enzyme can form homodimers, crosslinking experiments, SDS-PAGE
dimer
-
UmuD dimers exchange readily, and the subunits of UmuD2 and UmuD'2 exchange to form the UmuDD' heterodimer. The heterodimer is the preferred but not exclusive protein form, and both the heterodimer and homodimers exhibit slow exchange kinetics, which is further inhibited in the presence of interacting partner DinB
additional information
-
in addition to forming molecular dimers, the N-and C-terminal tails of UmuD' extend from a globular beta structure to associate and produce crystallized filaments. Higher oligomers are found in solution with UmuD' but not with UmuD nor with a mutant of UmuD' lacking the extended N terminus
additional information
-
UmuD proteins are shown to adopt multiple conformations in solution. UmuD contains only one cysteine (residue 24) per monomer at the cleavage site, which is between residues C24 and G25, cleavage of UmuD to form UmuD? removes the N-terminal 24 amino acids, which includes residue C24
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
proteolytic modification
full-length UmuD is expressed as a homodimer of 139-amino-acid subunits, which eventually cleaves its N-terminal 24 amino acids to form UmuD'. The cleavage product UmuD' and UmuC form the Y-family polymerase DNA Pol V (UmuD'2C) capable of performing translesion synthesis
proteolytic modification
UmuD is expressed as a 139-amino-acid protein, which eventually cleaves its N-terminal 24 amino acids to form UmuD'. Cleavage of UmuD to UmuD' dramatically affects the function of the protein and activates UmuC for translesion synthesis by forming DNA Polymerase V
proteolytic modification
-
inactive form UmuD is cleaved into active form UmuD'
proteolytic modification
-
inactive UmuD is posttranslationally activated by a RecA-mediated cleavage at its Gys24-Gly25 bond that yields UmuD', UmuD monomer is a better substrate for the cleavage reaction than the dimer
proteolytic modification
-
inactive UmuD is posttranslationally activated by a RecA-mediated cleavage that yields UmuD'
proteolytic modification
-
inactive UmuD is posttranslationally activated by a RecA-mediated cleavage that yields UmuD', P67D and P67R mutations of RecA result in reduced UmuD cleavage
proteolytic modification
-
processing of UmuD to the shorter, but mutagenically active UmuD' by activated RecA
proteolytic modification
-
processing of UmuD to the shorter, but mutagenically active UmuD' by ClpXP protease, UmuD' must form a heterodimer with its unabbreviated precursor for efficient degradation, UmuD2 homodimers are degraded with an efficiency similar to the UmuD' subunit of the UmuD/UmuD' heterodimer
proteolytic modification
-
RecA-facilitated cleavage of UmuD to UmuD' can be inhibited by overexpression of polymerase III subunits that interact with UmuD
proteolytic modification
-
RecA-facilitated cleavage of UmuD yields a carboxy-terminal fragment UmuD' that is active for mutagenesis, no other SOS gene products other than activated RecA are required for UmuD processing, high levels of activated RecA are required for cleavage in vivo
proteolytic modification
-
RecA-mediated posttranslational processing of UmuD to the shorter, but mutagenically active UmuD'
proteolytic modification
-
RecA-mediated posttranslational processing of UmuD to the shorter, but mutagenically active UmuD', K232A/E235A mutant of RecA cleaves UmuD more efficiently than wild-type RecA, T242A/R234A mutant of RecA is defective for cleavage of UmuD
proteolytic modification
-
UmuD is posttranslationally activated by a RecA-mediated cleavage that yields UmuD'
proteolytic modification
-
UmuD is posttranslationally activated by cleavage yielding UmuD'
proteolytic modification
-
UmuD protein is activated by a RecA-single-stranded DNA-facilitated self-cleavage event that serves to remove its amino-terminal 24 residues to yield UmuD'
proteolytic modification
-
slow auto-cleavage of UmuD2 to UmuD'2, the heterodimer efficiently cleaves to form UmuD'2
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F18A
decrease of induced mutagenesis to 20% of wild-type level, no cleavage of UmuD
N41D
the mutant generates stable, active UmuD and UmuD monomers that functionally mimic the dimeric wild type proteins. The mutant is proficient for cleavage and interacts physically with DNA polymerase IV (DinB) and the beta-clamp, facilitates UV-induced mutagenesis and promotes overall cell viability
P48G
expression of UmuD2 P48G is substantially lower than that of wild type UmuD2
S60A
T14A/F15A/F18A
decrease of induced mutagenesis to 20% of wild-type level, no cleavage of UmuD
V135S/K136A/R139A
expression of UmuD2 V135S/K136A/R139A is substantially lower than that of wild type UmuD2
A31C
C24A
C25D
-
site-directed mutagenesis, that removes the cleavage site Cys residue of UmuD, the mutation does not substantially affect UmuD function, cleavage site variant. For cleavage to occur, UmuD UmuD G25D dimer must first exchange in the presence of RecA:ssDNA, and any cleavage detected results from cleavage in trans. Cleavage is less efficient in this context, indicating that the decreased rate of cleavage in the trans dimers results from the time required for dimer exchange to first take place before cleavage can occur
D32C
-
deficiencies in RecA-mediated cleavage as well as in UV mutagenesis, less than 30% of the wild-type activity
D3A
-
the UmuD variant is non-cleavable but is a partial biological mimic of the cleaved form UmuD
D91K
-
site-directed mutagenesis, the mutation abolishes the interaction between the enzyme and the DNA polymerase III alpha subunit
E35C
-
deficiencies in RecA-mediated cleavage as well as in UV mutagenesis, less than 30% of the wild-type activity
F26A/P27A/S28A/P29A
-
can form heterodimers and is recognized by ClpXP protease
G65R
G92K
-
site-directed mutagenesis, the mutation abolishes the interaction between the enzyme and the DNA polymerase III alpha subunit
K97A
-
mutant is able to undergo intermolecular cleavage, but not intramolecular self-cleavage
L101G/R102G
-
mutant enzyme is defective in RecA-ssDNA-facilitated self-cleavage in vivo, can undergo RecA-ssDNA-facilitated cleavage in vitro, can interact directly with the RecA-ssDNA nucleoprotein filament in vitro, and is active in SOS mutagenesis in vivo
L40C
-
less than 30% of the wild-type activity, although defective in UV mutagenesis and in vitro RecA-mediated cleavage, mutant is able to be cleaved efficiently by RecA in vivo
L44C
L9A/R10A/E11A/I12A
-
heterodimer with UmuD' displays a significant increase in stability
N41D
-
site-directed mutagenesis, the monomeric UmuD N41D variant can only cleave in the cis conformation
P27S
Q23P/S60A
-
UmuD is non-cleavable via an intramolecular cleavage pathway, but it remains cleavable via the intermolecular pathway
R37A
-
when mutation is present in the UmuD' subunit of a UmuD/D' heterodimer it causes this subunit to be degraded substantially more slowly than its wild-type counterpart, when the mutation is present in the UmuD subunit of the heterodimer degradation of the UmuD' subunit occurs as efficiently as with the wild-type enzyme
S112C
-
4-azidoiodoacetanilide-modified mutant, cross-links moderately efficiently with RecA
S19C
-
4-azidoiodoacetanilide-modified mutant, almost no cross-linking with RecA
S57C
S60A
S60C
S67C
S81C
-
4-azidoiodoacetanilide-modified mutant, cross-links most efficiently with RecA
V34C
Y33C
-
less than 30% of the wild-type activity, although defective in UV mutagenesis and in vitro RecA-mediated cleavage, mutant is able to be cleaved efficiently by RecA in vivo
additional information
C24A
-
ability to participate in UV mutagenesis and RecA-mediated cleavage are similar to that of the wild-type enzyme
C24A
-
site-directed mutagenesis, that removes the cleavage site Cys residue of UmuD, the mutation does not substantially affect UmuD function, cleavage site variant
L44C
-
4-azidoiodoacetanilide-modified mutant, almost no cross-linking with RecA
S57C
-
4-azidoiodoacetanilide-modified mutant, cross-links moderately efficiently with RecA
S60A
-
site-directed mutagenesis, a non-cleavable mutant of UmuD and UmuD', inactive active site mutant. For cleavage to occur, UmuD S60A dimer must first exchange in the presence of RecA:ssDNA, and any cleavage detected results from cleavage in trans. Cleavage is less efficient in this context, indicating that the decreased rate of cleavage in the trans dimers results from the time required for dimer exchange to first take place before cleavage can occur
S60C
-
similar in iodoacetate reactivity but cross-links less efficiently by I2 oxidation than the wild-type enzyme, reduced activity in UV mutagenesis
S67C
-
4-azidoiodoacetanilide-modified mutant, cross-links moderately efficiently with RecA
V34C
-
4-azidoiodoacetanilide-modified mutant, cross-links most efficiently with RecA
additional information
characterization of two truncation variants of the Escherichia coli polymerase manager protein UmuD, UmuDELTA 8 (UmuD DELTA1-7) and UmuDELTA 18 (UmuS DELTA1-17). The loss of the N-terminal seven amino acids of UmuD results in changes in conformation of the N-terminal arms. UmuD 8 is cleaved as efficiently as full-length UmuD in vitro and in vivo, but expression of a plasmid-borne non-cleavable variant of UmuD 8 causes hypersensitivity to UV irradiation. UmuD 18 does not cleave to form UmuD', but confers resistance to UV radiation. Removal of the N-terminal seven residues of UmuD maintains its interactions with the alpha polymerase subunit of DNA polymerase III as well as its ability to disrupt interactions between alpha and the beta processivity clamp, whereas deletion of the N-terminal 17 residues results in decreases in binding to alpha and in the ability to disrupt the alpha-beta interaction. UmuD 8 mimics full-length UmuD in many respects, whereas UmuD 18 lacks a number of functions characteristic of UmuD. Deletion of the first eight residues does not change the cross-linking efficiency compared to UmuD. Deletion of the first 18 residues causes increased cross-linking efficiency, which is likely due to reduced interaction between the arms and the globular domain in the case of UmuD 18
additional information
-
characterization of two truncation variants of the Escherichia coli polymerase manager protein UmuD, UmuDELTA 8 (UmuD DELTA1-7) and UmuDELTA 18 (UmuS DELTA1-17). The loss of the N-terminal seven amino acids of UmuD results in changes in conformation of the N-terminal arms. UmuD 8 is cleaved as efficiently as full-length UmuD in vitro and in vivo, but expression of a plasmid-borne non-cleavable variant of UmuD 8 causes hypersensitivity to UV irradiation. UmuD 18 does not cleave to form UmuD', but confers resistance to UV radiation. Removal of the N-terminal seven residues of UmuD maintains its interactions with the alpha polymerase subunit of DNA polymerase III as well as its ability to disrupt interactions between alpha and the beta processivity clamp, whereas deletion of the N-terminal 17 residues results in decreases in binding to alpha and in the ability to disrupt the alpha-beta interaction. UmuD 8 mimics full-length UmuD in many respects, whereas UmuD 18 lacks a number of functions characteristic of UmuD. Deletion of the first eight residues does not change the cross-linking efficiency compared to UmuD. Deletion of the first 18 residues causes increased cross-linking efficiency, which is likely due to reduced interaction between the arms and the globular domain in the case of UmuD 18
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
highly purified UmuD is specifically degraded in vitro by Lon protease in an ATP-dependent manner, UmuD' is insensitive to proteolysis by Lon
-
highly purified UmuD/D' heterodimer is degraded in the presence of ATP, ClpP and ClpX, no degradation occurs when ClpX is omitted
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene umuD, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gonzalez, M.; Rasulova, F.; Maurizi, M.R.; Woodgate, R.
Subunit-specific degradation of the UmuD/D' heterodimer by the ClpXP protease: the role of trans recognition in UmuD' stability
EMBO J.
19
5251-5258
2000
Escherichia coli
Gonzalez, M.; Frank, E.G.; Levine, A.S.; Woodgate, R.
Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: in vitro degradation and identification of residues required for proteolysis
Genes Dev.
12
3889-3899
1998
Escherichia coli
Lee, M.H.; Ohta, T.; Walker, G.C.
A monocysteine approach for probing the structure and interactions of the UmuD protein
J. Bacteriol.
176
4825-4837
1994
Escherichia coli
Lee, M.H.; Walker, G.C.
Interactions of Escherichia coli UmuD with activated RecA analyzed by cross-linking UmuD monocysteine derivatives
J. Bacteriol.
178
7285-7294
1996
Escherichia coli
Guzzo, A.; Lee, M.H.; Oda, K.; Walker, G.C.
Analysis of the region between amino acids 30 and 42 of intact UmuD by a monocysteine approach
J. Bacteriol.
178
7295-7303
1996
Escherichia coli
Lee, M.H.; Guzzo, A.; Walker, G.C.
Inhibition of RecA-mediated cleavage in covalent dimers of UmuD
J. Bacteriol.
178
7304-7307
1996
Escherichia coli
Mustard, J.A.; Little, J.W.
Analysis of Escherichia coli RecA interactions with LexA, lambda CI, and UmuD by site-directed mutagenesis of recA
J. Bacteriol.
182
1659-1670
2000
Escherichia coli
Sutton, M.D.; Kim, M.; Walker, G.C.
Genetic and biochemical characterization of a novel umuD mutation: insights into a mechanism for UmuD self-cleavage
J. Bacteriol.
183
347-357
2001
Escherichia coli
Konola, J.T.; Guzzo, A.; Gow, J.B.; Walker, G.C.; Knight, K.L.
Differential cleavage of LexA and UmuD mediated by recA Pro67 mutants: implications for common LexA and UmuD binding sites on RecA
J. Mol. Biol.
276
405-415
1998
Escherichia coli
McDonald, J.P.; Maury, E.E.; Levine, A.S.; Woodgate, R.
Regulation of UmuD cleavage: role of the amino-terminal tail
J. Mol. Biol.
282
721-730
1998
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
Woodgate, R.; Ennis, D.G.
Levels of chromosomally encoded Umu proteins and requirements for in vivo UmuD cleavage
Mol. Gen. Genet.
229
10-16
1991
Escherichia coli
Koch, W.H.; Ennis, D.G.; Levine, A.S.; Woodgate, R.
Escherichia coli umuDC mutants: DNA sequence alterations and UmuD cleavage
Mol. Gen. Genet.
233
443-448
1992
Escherichia coli
Neher, S.B.; Sauer, R.T.; Baker, T.A.
Distinct peptide signals in the UmuD and UmuD' subunits of UmuD/D' mediate tethering and substrate processing by the ClpXP protease
Proc. Natl. Acad. Sci. USA
100
13219-13224
2003
Escherichia coli
Shinagawa, H.; Iwasaki, H.; Kato, T.; Nakata, A.
RecA protein-dependent cleavage of UmuD protein and SOS mutagenesis
Proc. Natl. Acad. Sci. USA
85
1806-1810
1988
Escherichia coli
Battista, J.R.; Ohta, T.; Nohmi, T.; Sun, W.; Walker, G.C.
Dominant negative umuD mutations decreasing RecA-mediated cleavage suggest roles for intact UmuD in modulation of SOS mutagenesis
Proc. Natl. Acad. Sci. USA
87
7190-7194
1990
Escherichia coli
Sutton, M.D.; Opperman, T.; Walker, G.C.
The Escherichia coli SOS mutagenesis proteins UmuD and UmuD' interact physically with the replicative DNA polymerase
Proc. Natl. Acad. Sci. USA
96
12373-12378
1999
Escherichia coli
Peat, T.S.; Frank, E.G.; McDonald, J.P.; Levine, A.S.; Woodgate, R.; Hendrickson, W.A.
The UmuD' protein filament and its potential role in damage induced mutagenesis
Structure
4
1401-1412
1996
Escherichia coli
Duzen Jill , D.J.; Walker Graham , W.G.; Sutton Mark , S.M.
Identification of specific amino acid residues in the E. coli beta processivity clamp involved in interactions with DNA polymerase III, UmuD and UmuD
DNA Repair
3
301-312
2004
Escherichia coli
Bridges, B.A.
Error-prone repair and translesion synthesis III: The activation of UmuD (or less is more)
DNA Repair
4
1047-1059
2005
Escherichia coli
Paetzel, M.; Woodgate, R.
UmuD and UmuD proteins
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. )Academic Press
2
1976-1981
2004
Escherichia coli, Pseudomonas syringae, Salmonella enterica subsp. enterica serovar Typhimurium
-
Paetzel, M.; Woodgate, R.
UmuD and UmuD proteins
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner; J. F. , eds. )Academic Press
2
1976-1981
2004
Escherichia coli
-
Beuning Penny , B.P.; Simon Sharotka , S.S.; Zemla Ada, Z.A.; Barsky Danie, B.D.; Walker Graham , W.G.
A non-cleavable UmuD variant that acts as a UmuD mimic
J. Biol. Chem.
281
9633-9640
2006
Escherichia coli (P0AG11), Escherichia coli
Godoy, V.G.; Jarosz, D.F.; Simon, S.M.; Abyzov, A.; Ilyin, V.; Walker, G.C.
UmuD and RecA directly modulate the mutagenic potential of the Y family DNA polymerase DinB
Mol. Cell
28
1058-1070
2007
Escherichia coli (P0AG11), Escherichia coli FC40 (P0AG11)
Simon, S.M.; Sousa, F.J.; Mohana-Borges, R.; Walker, G.C.
Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products
Proc. Natl. Acad. Sci. USA
105
1152-1157
2008
Escherichia coli
Jiang, Q.; Karata, K.; Woodgate, R.; Cox, M.M.; Goodman, M.F.
The active form of DNA polymerase V is UmuD(2)C-RecA-ATP
Nature
460
359-363
2009
Escherichia coli
Foti, J.J.; Delucia, A.M.; Joyce, C.M.; Walker, G.C.
UmuD2 inhibits a non-covalent step during DinB-mediated template slippage on homopolymeric nucleotide runs
J. Biol. Chem.
285
23086-23095
2010
Escherichia coli
Fang, J.; Rand, K.D.; Silva, M.C.; Wales, T.E.; Engen, J.R.; Beuning, P.J.
Conformational dynamics of the Escherichia coli DNA polymerase manager proteins UmuD and UmuD
J. Mol. Biol.
398
40-53
2010
Escherichia coli
Ollivierre, J.N.; Sikora, J.L.; Beuning, P.J.
The dimeric SOS mutagenesis protein UmuD is active as a monomer
J. Biol. Chem.
286
3607-3617
2011
Escherichia coli (P0AG11), Escherichia coli
Ollivierre, J.N.; Fang, J.; Beuning, P.J.
The roles of UmuD in regulating mutagenesis
J. Nucleic Acids
2010
pii: 947680
2010
Escherichia coli
Ollivierre, J.N.; Budil, D.E.; Beuning, P.J.
Electron spin labeling reveals the highly dynamic N-terminal arms of the SOS mutagenesis protein UmuD
Mol. Biosyst.
7
3183-3186
2011
Escherichia coli
Ollivierre, J.N.; Sikora, J.L.; Beuning, P.J.
Dimer exchange and cleavage specificity of the DNA damage response protein UmuD
Biochim. Biophys. Acta
1834
611-620
2013
Escherichia coli, Escherichia coli AB1157
Hare, J.M.; Adhikari, S.; Lambert, K.V.; Hare, A.E.; Grice, A.N.
The Acinetobacter regulatory UmuDAb protein cleaves in response to DNA damage with chimeric LexA/UmuD characteristics
FEMS Microbiol. Lett.
334
57-65
2012
Escherichia coli, Acinetobacter baylyi
Chaurasiya, K.R.; Ruslie, C.; Silva, M.C.; Voortman, L.; Nevin, P.; Lone, S.; Beuning, P.J.; Williams, M.C.
Polymerase manager protein UmuD directly regulates Escherichia coli DNA polymerase III alpha binding to ssDNA
Nucleic Acids Res.
41
8959-8968
2013
Escherichia coli
Murison, D.A.; Timson, R.C.; Koleva, B.N.; Ordazzo, M.; Beuning, P.J.
Identification of the dimer exchange interface of the bacterial DNA damage response protein UmuD
Biochemistry
56
4773-4785
2017
Escherichia coli (P0AG11), Escherichia coli, Escherichia coli K12 (P0AG11)
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