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J Bacteriol. 2006 Feb;188(4):1663-6.

Repressor of phage 16-3 with altered binding specificity indicates spatial differences in repressor-operator complexes.

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1
Institute of Genetics, Agricultural Biotechnology Center, Gödöllõ, Szent-Györgyi A. 4., H-2100, Hungary.

Abstract

The C repressor protein of phage 16-3, which is required for establishing and maintaining lysogeny, recognizes structurally different operators which differ by 2 bp in the length of the spacer between the conserved palindromic sequences. A "rotationally flexible protein homodimers" model has been proposed in order to explain the conformational adaptivity of the 16-3 repressor. In this paper, we report on the isolation of a repressor mutant with altered binding specificity which was used to identify a residue-base pair contact and to monitor the spatial relationship of the recognition helix of C repressor to the contacting major groove of DNA within the two kinds of repressor-operator complexes. Our results indicate spatial differences at the interface which may reflect different docking arrangements in recognition of the structurally different operators by the 16-3 repressor.

PMID:
16452452
PMCID:
PMC1367245
DOI:
10.1128/JB.188.4.1663-1666.2006
[Indexed for MEDLINE]
Free PMC Article
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