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Acquired Immunodeficiency Syndrome
Requirements for bypass of UV-induced lesions in single-stranded DNA of bacteriophage phi X174 in Salmonella typhimurium.
Adenoviridae Infections
Degradation of a novel DNA damage response protein, tankyrase 1 binding protein 1 (Tab182), following adenovirus infection.
Ataxia
DNA damage-induced ATM- and Rad-3-related (ATR) kinase activation in non-replicating cells is regulated by the XPB subunit of transcription factor IIH (TFIIH).
Ataxia Telangiectasia
Ataxia Telangiectasia Mutated Kinase Mediates NF-?B Serine 276 Phosphorylation and Interferon Expression via the IRF7-RIG-I Amplification Loop in Paramyxovirus Infection.
Ataxia Telangiectasia
ATM Promotes RAD51-Mediated Meiotic DSB Repair by Inter-Sister-Chromatid Recombination in Arabidopsis.
Ataxia Telangiectasia
ATR inhibition sensitizes HPV- and HPV+ head and neck squamous cell carcinoma to cisplatin.
Ataxia Telangiectasia
Heart failure and diabetes: role of ATM.
Ataxia Telangiectasia
The Major Tegument Protein of Bovine Herpesvirus 1, VP8, Interacts with DNA Damage Response Proteins and Induces Apoptosis.
Breast Neoplasms
Clinical and biological significance of RAD51 expression in breast cancer: a key DNA damage response protein.
Breast Neoplasms
Filamin A inhibits tumor progression through regulating BRCA1 expression in human breast cancer.
Breast Neoplasms
Prognostic effects of abnormal DNA damage response protein expression in breast cancer.
Carcinoma
Association of amino acid substitution polymorphisms in DNA repair genes TP53, POLI, REV1 and LIG4 with lung cancer risk.
Carcinoma
ATR inhibition sensitizes HPV- and HPV+ head and neck squamous cell carcinoma to cisplatin.
Carcinoma, Squamous Cell
Association of amino acid substitution polymorphisms in DNA repair genes TP53, POLI, REV1 and LIG4 with lung cancer risk.
Carcinoma, Squamous Cell
ATR inhibition sensitizes HPV- and HPV+ head and neck squamous cell carcinoma to cisplatin.
Fanconi Anemia
A UAF1-containing multisubunit protein complex regulates the Fanconi anemia pathway.
Glioblastoma
Constitutive CHK1 expression drives a pSTAT3-CIP2A circuit that promotes glioblastoma cell survival and growth.
Leiomyoma
Immunofluorescence analysis of DNA damage response protein p53-binding protein 1 in a case of uterine dedifferentiated leiomyosarcoma arising from leiomyoma.
Leiomyosarcoma
Immunofluorescence analysis of DNA damage response protein p53-binding protein 1 in a case of uterine dedifferentiated leiomyosarcoma arising from leiomyoma.
Leukemia
The Epstein-Barr virus nuclear antigen-1 promotes telomere dysfunction via induction of oxidative stress.
Liver Neoplasms
DNA Damage Response Protein CHK2 Regulates Metabolism in Liver Cancer.
Lung Neoplasms
Role of ATF-2 in regulation of epithelial-mesenchymal transition and radio-sensitivity of A549 cells mediated by secreted soluble factors.
Neoplasms
Bringing H2AX into the angiogenesis family.
Neoplasms
Filamin A inhibits tumor progression through regulating BRCA1 expression in human breast cancer.
Neoplasms
Immunofluorescence analysis of DNA damage response protein p53-binding protein 1 in a case of uterine dedifferentiated leiomyosarcoma arising from leiomyoma.
Neoplasms
Loss of the retinoblastoma tumor suppressor correlates with improved outcome in patients with lung adenocarcinoma treated with surgery and chemotherapy.
Neoplasms
Multi-omics analysis reveals neoantigen-independent immune cell infiltration in copy-number driven cancers.
Neoplasms
Prognostic effects of abnormal DNA damage response protein expression in breast cancer.
Neoplasms
Role of ATF-2 in regulation of epithelial-mesenchymal transition and radio-sensitivity of A549 cells mediated by secreted soluble factors.
Neoplasms
Yeast-based screening of cancer mutations in the DNA damage response protein Mre11 demonstrates importance of conserved capping domain residues.
Nijmegen Breakage Syndrome
The Major Tegument Protein of Bovine Herpesvirus 1, VP8, Interacts with DNA Damage Response Proteins and Induces Apoptosis.
Ovarian Neoplasms
Integration of computer-aided automated analysis algorithms in the development and validation of immunohistochemistry biomarkers in ovarian cancer.
Prostatic Neoplasms
Targeted radiosensitization of ETS fusion-positive prostate cancer through PARP1 inhibition.
Squamous Cell Carcinoma of Head and Neck
ATR inhibition sensitizes HPV- and HPV+ head and neck squamous cell carcinoma to cisplatin.
Triple Negative Breast Neoplasms
Prognostic effects of abnormal DNA damage response protein expression in breast cancer.
umud protein deficiency
Methyl methanesulphonate (MMS) is clearly mutagenic in S. typhimurium strain TA1535; a comparison with strain TA100.
Urinary Bladder Neoplasms
Attenuated XPC expression is not associated with impaired DNA repair in bladder cancer.
Xeroderma Pigmentosum
Attenuated XPC expression is not associated with impaired DNA repair in bladder cancer.
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metabolism
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competition between enzyme UmuD and ssDNA for DNA polymerase III alpha binding is a distinct mechanism for polymerase exchange
malfunction
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effects of recA and umuD mutations on UmuDAb cleavage in DNA damage response of Escherichia coli
malfunction
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effects of recA and umuD mutations on UmuDAb cleavage in DNA damage response of Escherichia coli
malfunction
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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
malfunction
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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
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physiological function
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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
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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
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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
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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
UmuD regulates the cellular response to DNA damage
physiological function
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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
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in the DNA damage response, UmuD forms part of the error-prone (UmuD'2)C polymerase V, and is activated for this function by self-cleavage after DNA damage. The umuD homologue umuDAb regulates transcription of DNA-damage induced genes. DNA damage from mitomycin C or UV exposure causes UmuDAb cleavage in both Escherichia coli wild-type and DELTAumuD cells on a timescale resembling UmuD, but does not require UmuD. UmuD and UmuDAb require RecA for cleavage
physiological function
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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
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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
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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
physiological function
the plasmid (pUM505)-encoded UmuD homologue regulates expression of Pseudomonas aeruginosa SOS genes. The UmuDpR protein is a repressor of Pseudomonas aeruginosa SOS genes controlled by LexA
physiological function
the umuD gene products are upregulated after DNA damage and play roles in both nonmutagenic and mutagenic aspects of the SOS response
physiological function
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the umuD gene products are upregulated after DNA damage and play roles in both nonmutagenic and mutagenic aspects of the SOS response
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physiological function
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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
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additional information
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Acinetobacter UmuDAb possesses both the conserved serine-lysine catalytic dyad required by UmuD, LexA, and some bacteriophage repressors for self-cleavage as well as the (Ala/Cys)-Gly cleavage site
additional information
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intermolecular mechanism of UmuD self-cleavage of enzyme dimers, overview
additional information
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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
additional information
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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
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proteolytic modification
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inactive form UmuD is cleaved into active form UmuD'
proteolytic modification
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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
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inactive UmuD is posttranslationally activated by a RecA-mediated cleavage that yields UmuD'
proteolytic modification
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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
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processing of UmuD to the shorter, but mutagenically active UmuD' by activated RecA
proteolytic modification
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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
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RecA-facilitated cleavage of UmuD to UmuD' can be inhibited by overexpression of polymerase III subunits that interact with UmuD
proteolytic modification
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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
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RecA-mediated posttranslational processing of UmuD to the shorter, but mutagenically active UmuD'
proteolytic modification
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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
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UmuD is posttranslationally activated by a RecA-mediated cleavage that yields UmuD'
proteolytic modification
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UmuD is posttranslationally activated by cleavage yielding UmuD'
proteolytic modification
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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
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slow auto-cleavage of UmuD2 to UmuD'2, the heterodimer efficiently cleaves to form UmuD'2
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
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slow auto-cleavage of UmuD2 to UmuD'2, the heterodimer efficiently cleaves to form UmuD'2
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proteolytic modification
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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
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proteolytic modification
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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
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proteolytic modification
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RecA-mediated posttranslational processing of UmuD to the shorter, but mutagenically active UmuD', Salmonella typhimurium UmuD is processed at a significantly faster rate than the Escherichia coli protein, enhanced cleavage can be attributed to the presence of a Pro23 residue
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A83X
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the site-directed mutation of UmuDAb at Ala83 abolishes cleavage activity
K156X
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the site-directed mutation of UmuDAb at Lys156 abolishes cleavage activity
S119X
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the site-directed mutation of UmuDAb at Ser119 abolishes cleavage activity
A30T
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substantial extent of proteolytic cleavage
A7C/C24A/S60A
variant with maximal cross-linking
A89C
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reduced ability to for a heterodimer with UmuD'
C24Y
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poor extent of proteolytic cleavage
C25D
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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
D126C
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reduced ability to form a homodimer and a heterodimer with UmuD'
D20Y
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slight increase in activation rate by cleavage
D32C
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deficiencies in RecA-mediated cleavage as well as in UV mutagenesis, less than 30% of the wild-type activity
D3A
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the UmuD variant is non-cleavable but is a partial biological mimic of the cleaved form UmuD
D91A
the mutant is soluble and purifies as the wild type UmuD
D91K
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site-directed mutagenesis, the mutation abolishes the interaction between the enzyme and the DNA polymerase III alpha subunit
E11V/I12V/V13K
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supports ClpXP degradation of UmuD'
E35C
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deficiencies in RecA-mediated cleavage as well as in UV mutagenesis, less than 30% of the wild-type activity
F15A
slight decrease of induced mutagenesis compared to wild-type
F15L
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no change in activation rate by cleavage
F18A
decrease of induced mutagenesis to 20% of wild-type level, no cleavage of UmuD
F26A/P27A/S28A/P29A
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can form heterodimers and is recognized by ClpXP protease
G129D
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poor extent of proteolytic cleavage
G25D
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medium extent of proteolytic cleavage
G25S
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poor extent of proteolytic cleavage
G92C
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site-directed mutagenesis of of UmuD'
G92D
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substantial extent of proteolytic cleavage
G92K
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site-directed mutagenesis, the mutation abolishes the interaction between the enzyme and the DNA polymerase III alpha subunit
G92N
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defective for RecA-mediated UmuD cleavage
I38C
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poor reaction with iodoacetate
I4F
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slight increase in activation rate by cleavage
K97A
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mutant is able to undergo intermolecular cleavage, but not intramolecular self-cleavage
L101G/R102G
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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
L107F
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substantial extent of proteolytic cleavage
L17F
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no change in activation rate by cleavage
L40C
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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
L9A/R10A/E11A/I12A
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heterodimer with UmuD' displays a significant increase in stability
P48G
expression of UmuD2 P48G is substantially lower than that of wild type UmuD2
Q23P
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mutant phenotype is reminiscent of the wild-type
Q23P/S60A
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UmuD is non-cleavable via an intramolecular cleavage pathway, but it remains cleavable via the intermolecular pathway
R37A
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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
R37C
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poor reaction with iodoacetate
S112C
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4-azidoiodoacetanilide-modified mutant, cross-links moderately efficiently with RecA
S19C
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4-azidoiodoacetanilide-modified mutant, almost no cross-linking with RecA
S81C
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4-azidoiodoacetanilide-modified mutant, cross-links most efficiently with RecA
T14A
slight decrease of induced mutagenesis compared to wild-type
T14A/F15A/F18A
decrease of induced mutagenesis to 20% of wild-type level, no cleavage of UmuD
T14A/L17A/F18A
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the mutant is a non-cleavable variant of UmuD
T14P
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no change in activation rate by cleavage
T95M
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substantial extent of proteolytic cleavage
V135S/K136A/R139A
expression of UmuD2 V135S/K136A/R139A is substantially lower than that of wild type UmuD2
Y33C
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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
C24A
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site-directed mutagenesis, that removes the cleavage site Cys residue of UmuD, the mutation does not substantially affect UmuD function, cleavage site variant
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C25D
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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
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G92C
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site-directed mutagenesis of of UmuD'
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N41D
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site-directed mutagenesis, the monomeric UmuD N41D variant can only cleave in the cis conformation
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S60A
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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
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D91A
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the mutant is soluble and purifies as the wild type UmuD
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S60A
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noncleavable UmuD variant
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A7C/C24A/S60A
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variant with maximal cross-linking
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S60A
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non-cleavage variant
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A31C
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partial reduction in UV mutability
C24A
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ability to participate in UV mutagenesis and RecA-mediated cleavage are similar to that of the wild-type enzyme
C24A
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site-directed mutagenesis, that removes the cleavage site Cys residue of UmuD, the mutation does not substantially affect UmuD function, cleavage site variant
G65R
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defective for RecA-mediated UmuD cleavage
G65R
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medium extent of proteolytic cleavage
L44C
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4-azidoiodoacetanilide-modified mutant, almost no cross-linking with RecA
L44C
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reduced ability to form a homodimer
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
N41D
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site-directed mutagenesis, the monomeric UmuD N41D variant can only cleave in the cis conformation
P27S
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defective for RecA-mediated UmuD cleavage
P27S
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substantial extent of proteolytic cleavage
S57C
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4-azidoiodoacetanilide-modified mutant, cross-links moderately efficiently with RecA
S57C
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reduced activity in UV mutagenesis
S60A
noncleavable UmuD variant
S60A
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active-site UmuD mutant
S60A
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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
S60A
non-cleavage variant
S60C
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4-azidoiodoacetanilide-modified mutant, no cross-linking with RecA
S60C
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similar in iodoacetate reactivity but cross-links less efficiently by I2 oxidation than the wild-type enzyme, reduced activity in UV mutagenesis
S67C
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4-azidoiodoacetanilide-modified mutant, cross-links moderately efficiently with RecA
S67C
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only 9% as active as the wild-type enzyme in UV mutagenesis
V34C
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4-azidoiodoacetanilide-modified mutant, cross-links most efficiently with RecA
V34C
-
defective for RecA-mediated cleavage
V34C
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reduced activity in UV mutagenesis
additional information
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generation of isogenic mutant UmuDC homologues A1S_0636-A1S_0637, A1S_1174-A1S_1173, and A1S_1389, the mutants are less able to acquire resistance to rifampin and streptomycin through the activities of their error-prone DNA polymerase, but neither the growth rate nor the UV-related survival of any of the three mutants is significantly different from that of the wild-type parental strain
additional information
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generation of isogenic mutant UmuDC homologues A1S_0636-A1S_0637, A1S_1174-A1S_1173, and A1S_1389, the mutants are less able to acquire resistance to rifampin and streptomycin through the activities of their error-prone DNA polymerase, but neither the growth rate nor the UV-related survival of any of the three mutants is significantly different from that of the wild-type parental strain
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additional information
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generation of DELTAumuD mutant cells
additional information
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generation of DELTAumuD mutant cells
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
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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
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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
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