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EC Number
General Information
Commentary
Reference
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
metabolism
competition between enzyme UmuD and ssDNA for DNA polymerase III alpha binding is a distinct mechanism for polymerase exchange
more
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
more
intermolecular mechanism of UmuD self-cleavage of enzyme dimers, overview
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
physiological function
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
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
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
Results 1 - 10 of 16 > >>