Author/Editor		Butala, Matej; Hodošček, Milan; Anderluh, Gregor; Podlesek, Zdravko; Žgur-Bertok, Darja
Title		Intradomain LexA rotation is a prerequisite for DNA binding specificity
Type		članek
Source		Febs Lett
Vol. and No.		Letnik 581, št. 25
Publication year		2007
Volume		str. 4816-20
Language		eng
Abstract		In the absence of DNA damage the LexA protein represses the bacterial SOS system. We performed molecular dynamic simulations of two LexA dimers bound to operators. Our model predicted that rotation of the LexA DNA binding domain, with respect to the dimerised C-terminal domain, is required for selective DNA binding. To confirm the model, double and quadruple cysteine LexA mutants were engineered. Electrophoretic mobility-shift assay and surface plasmon resonance showed that disulfide bond formation between the introduced cysteine residues precluded LexA specific DNA binding due to blocked domain reorientation. Our model could provide the basis for novel drug design.
Descriptors		COMPUTER SIMULATION TRANSCRIPTION, GENETIC DNA-BINDING PROTEINS REPRESSOR PROTEINS PLASMIDS ESCHERICHIA COLI MUTATION