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

Szilamér Ferenczi, L. Orosz, Péter P. Papp

Research output: Contribution to journalArticle

Abstract

The C repressor protein of phage 16-3, which is required for establishing and maintaining lysogeny, recognizes structurally diferent 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.

Original languageEnglish
Pages (from-to)1663-1666
Number of pages4
JournalJournal of Bacteriology
Volume188
Issue number4
DOIs
Publication statusPublished - Feb 2006

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Lysogeny
Conserved Sequence
Base Pairing
Bacteriophages
DNA
Proteins
phage repressor proteins

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

Repressor of phage 16-3 with altered binding specificity indicates spatial differences in repressor-operator complexes. / Ferenczi, Szilamér; Orosz, L.; Papp, Péter P.

In: Journal of Bacteriology, Vol. 188, No. 4, 02.2006, p. 1663-1666.

Research output: Contribution to journalArticle

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