Figure 1.
LexA auto-cleavage fragments are captured and degraded by ClpXP. (A) Western blot of the LexA species captured by the ClpPtrap and generated by auto-cleavage in vitro. (B) The proteolytic stability of LexA, LexA1–84, and LexA85–202 in vivo was determined in clpX+ (MC4100) and clpX− (SG22101) strains bearing plasmid pJL42. LexA, LexA1–84, and LexA85–202 were identified by comparison with auto-cleaved LexA (lane S). It is difficult to see the continued disappearance of LexA, as expected from auto-processing, because the Western blots are mildly overexposed to allow observation of the low levels of LexA85–202. (C) ClpXP degradation of purified LexA, LexA1–84, and LexA85–202 in vitro. The band marked ATP-RS is creatine kinase.