EC Number |
General Information |
Reference |
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3.4.21.B30 | 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 |
705887 |
3.4.21.B30 | 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 |
709122 |
3.4.21.B30 | 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. |
709543 |
3.4.21.B30 | physiological function |
UmuD regulates the cellular response to DNA damage |
717851 |
3.4.21.B30 | 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 |
718023 |
3.4.21.B30 | 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 |
718102 |
3.4.21.B30 | 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 |
-, 731345 |
3.4.21.B30 | more |
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 |
-, 731345 |
3.4.21.B30 | 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 |
-, 731345 |
3.4.21.B30 | malfunction |
effects of recA and umuD mutations on UmuDAb cleavage in DNA damage response of Escherichia coli |
731823 |