Abstract：
:During the SOS response, LexA repressor is inactivated by specific cleavage. Although cleavage requires RecA protein in vivo, RecA acts indirectly as a coprotease by stimulating an inherent self-cleavage activity of LexA. In lambda lysogens, cleavage of lambda Cl repressor in a similar but far slower reaction results in prophage induction. We describe an intermolecular cleavage reaction in which the C-terminal fragment of LexA acted as an enzyme to cleave other molecules of LexA. The C-terminal fragment of lambda repressor cleaved the LexA substrates about as efficiently as did the LexA enzyme, suggesting that the slow rate of Cl self-cleavage results from a weak interaction between its cleavage site and the active site.
journal_name
Celljournal_title
Cellauthors
Kim B,Little JWdoi
10.1016/0092-8674(93)90645-7subject
Has Abstractpub_date
1993-06-18 00:00:00pages
1165-73issue
6eissn
0092-8674issn
1097-4172pii
0092-8674(93)90645-7journal_volume
73pub_type
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