Little J W
Department of Biochemistry, University of Arizona, Tucson 85721.
Biochimie. 1991 Apr;73(4):411-21. doi: 10.1016/0300-9084(91)90108-d.
Specific LexA cleavage can occur under two different conditions: RecA-mediated cleavage requires an activated form of RecA, while an intramolecular self-cleavage termed autodigestion proceeds spontaneously at high pH and does not involve RecA. The two cleavage reactions are closely related. We postulate that RecA stimulates autodigestion rather than acting as a typical protease, and it is proposed to term this activity 'RecA coprotease' to emphasize this indirect role. The mechanism of autodigestion is similar to that of a serine protease, and RecA appears to act by reducing the pKa of a critical lysine residue LexA. A new class of mutants, termed lexA (IndS), is described; these mutations increase the rate of LexA cleavage.
特异性LexA切割可在两种不同条件下发生:RecA介导的切割需要活化形式的RecA,而一种称为自消化的分子内自我切割在高pH下自发进行,且不涉及RecA。这两种切割反应密切相关。我们推测RecA刺激自消化而非作为典型的蛋白酶起作用,并且建议将这种活性称为“RecA共蛋白酶”以强调这种间接作用。自消化机制类似于丝氨酸蛋白酶,并且RecA似乎通过降低关键赖氨酸残基LexA的pKa起作用。描述了一类新的突变体,称为lexA(IndS);这些突变增加了LexA切割的速率。