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 Previous Article

Journal of Bacteriology, February 2006, p. 1663-1666, Vol. 188, No. 4
0021-9193/06/$08.00+0     doi:10.1128/JB.188.4.1663-1666.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

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

Szilamér Ferenczi,1 László Orosz,1,2 and Péter P. Papp1*

Institute of Genetics, Agricultural Biotechnology Center, Gödöllõ, Szent-Györgyi A. 4., H-2100, Hungary,1 Department of Genetics, Eötvös Loránd University and Research Group for Molecular Genetics of the Hungarian Academy of Sciences, Pázmány P. Sétány 1/C, H-1117, Budapest, Hungary2

Received 23 September 2005/ Accepted 23 November 2005

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.

* Corresponding author. Mailing address: Institute of Genetics, Agricultural Biotechnology Center, Gödöllõ, Szent-Györgyi A. 4., H-2100, Hungary. Phone: 36 (28)-526-106, Fax: 36 (28)-526-145. E-mail: ppapp{at}abc.hu.

Journal of Bacteriology, February 2006, p. 1663-1666, Vol. 188, No. 4
0021-9193/06/$08.00+0     doi:10.1128/JB.188.4.1663-1666.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.





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