2013
DOI: 10.1016/j.bbapap.2012.11.008
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Dimer exchange and cleavage specificity of the DNA damage response protein UmuD

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Cited by 10 publications
(35 citation statements)
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“…A similar rearrangement was recently demonstrated under equilibrium conditions in vitro , confirming that formation of the heterodimeric UmuD/D′ complex is preferred over homodimeric UmuD 2 or UmuD′ 2 [34]. The fact that formation of a UmuD/D′ heterodimer is preferred over formation of homodimers and that UmuD′ becomes susceptible to degradation by ClpXP only when it is part of the heterodimeric complex with UmuD provides a mechanism whereby E.coli can reduce the intracellular levels of the Umu proteins after they have facilitated survival of the damaged cell.…”
Section: Umud-umud′ Heterodimerization and Clpxp Proteolysissupporting
confidence: 80%
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“…A similar rearrangement was recently demonstrated under equilibrium conditions in vitro , confirming that formation of the heterodimeric UmuD/D′ complex is preferred over homodimeric UmuD 2 or UmuD′ 2 [34]. The fact that formation of a UmuD/D′ heterodimer is preferred over formation of homodimers and that UmuD′ becomes susceptible to degradation by ClpXP only when it is part of the heterodimeric complex with UmuD provides a mechanism whereby E.coli can reduce the intracellular levels of the Umu proteins after they have facilitated survival of the damaged cell.…”
Section: Umud-umud′ Heterodimerization and Clpxp Proteolysissupporting
confidence: 80%
“…It seems unlikely that cleavage of the N-terminal tail of the two UmuD protomers occurs simultaneously, meaning that the proteins would exist as a heterodimer of intact UmuD and processed UmuD′, until such time that the tail of the intact UmuD protomer is eventually processed to form homodimeric UmuD′ [34] (Fig. 2).…”
Section: Umud-umud′ Heterodimerization and Clpxp Proteolysismentioning
confidence: 99%
“…Furthermore, the UmuD G92D mutation is poorly cleavable, but when this mutation was constructed in the context of UmuD′, cells harboring this variant were mutable to a similar extent as cells harboring wild-type UmuD (50,51), suggesting that the G92D mutation does not alter the ability of UmuD′ to facilitate UmuC-dependent mutagenesis. On the other hand, the UmuD G92C variant was as proficient for cleavage as wild-type UmuD (52). Therefore, this region of UmuD seems to be an important site for a number of protein interactions.…”
Section: Discussionmentioning
confidence: 91%
“…The SOS mutator effect depends on cleavage of both LexA, determining the expression level of the umuDC operon, and UmuD. The latter cleavage yields UmuD′, which is an essential component of the Pol V mutasome ( 14 , 42 43 ). Thus, in principle, the inhibitory effect exerted by the ndk and dcd deficiencies in the lex + background could be due to an inhibition of both cleavages.…”
Section: Resultsmentioning
confidence: 99%