Repressor of Phage 16-3 with Altered Binding Specificity Indicates Spatial Differences in Repressor-Operator Complexes

Ferenczi, Szilamér and Orosz, László and Papp, P. Péter (2006) Repressor of Phage 16-3 with Altered Binding Specificity Indicates Spatial Differences in Repressor-Operator Complexes. Journal of Bacteriology, 188 (4). pp. 1663-1666. ISSN 0021-9193 (print), 1098-5530 (online)

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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.

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