Journal
GENES & DEVELOPMENT
Volume 17, Issue 9, Pages 1084-1089Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.1078003
Keywords
SOS response; proteolysis; AAA(+); peptide recognition; ClpP; UV response
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Funding
- NIAID NIH HHS [R01 AI016892, AI-16892] Funding Source: Medline
- NIGMS NIH HHS [R01 GM049224, R01 GM049224-11] Funding Source: Medline
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The DNA-damage response genes in bacteria are upregulated when LexA repressor undergoes autocatalytic cleavage stimulated by activated RecA protein. Intact LexA is stable to intracellular degradation but its auto-cleavage fragments are degraded rapidly. Here, both fragments of LexA are shown to be substrates for the ClpXP protease. ClpXP recognizes these fragments using sequence motifs that flank the auto-cleavage site but are dormant in intact LexA. Furthermore, ClpXP degradation of the LexA-DNA-binding fragment is important to cell survival after DNA damage. These results demonstrate how one protein-processing event can activate latent protease recognition signals, triggering a cascade of protein turnover in response to environmental stress.
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