RecA-Dependent Cleavage of LexA Dimers

A critical step in the SOS response of Escherichia coli is the specific proteolytic cleavage of the LexA repressor. This reaction is catalyzed by an activated form of RecA, acting as a co-protease to stimulate the self-cleavage activity of LexA. This process has been reexamined in light of evidence...

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Veröffentlicht in:	Journal of molecular biology 2008-03, Vol.377 (1), p.148-161
Hauptverfasser:	Giese, Kim C., Michalowski, Christine B., Little, John W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Alanine Bacterial Proteins - chemistry Bacterial Proteins - metabolism Cross-Linking Reagents Cyclic AMP-Dependent Protein Kinases dimer Dimerization Escherichia coli Escherichia coli - enzymology Kinetics LexA Lysine Mutant Proteins Protein Conformation Rec A Recombinases - metabolism RecA Serine Endopeptidases - chemistry Serine Endopeptidases - metabolism SOS specific cleavage Thermodynamics
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