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PMID: 3430609 Published · ppublish English Journal Article

Characterization of the binding sites of c1 repressor of bacteriophage P1. Evidence for multiple asymmetric sites.

Journal of molecular biology ·Vol. 198 ·No. 2 ·1987-11-20 ·Pages 281-93

Eliason JL, Sternberg N

Abstract

The repressor of bacteriophage P1, encoded by the c1 gene, is responsible for maintaining a P1 prophage in the lysogenic state. In this paper we present: (1) the sequence of the rightmost 943 base-pairs of the P1 genetic map that includes the 5'-terminal 224 base-pairs of the c1 gene plus its upstream region; (2) the construction of a plasmid that directs the production of approximately 5% of the cell's protein as P1 repressor; (3) a deletion analysis that establishes the startpoint of P1 repressor translation; (4) filter binding experiments that demonstrate that P1 repressor binds to several regions upstream from the c1 gene; (5) DNase I footprint experiments that directly identify two of the P1 repressor binding sites. Sequences very similar to the identified binding sites occur in at least 11 sites in P1, in most cases near functions known, or likely, to be controlled by repressor. From these sites we have derived the consensus binding site sequence ATTGCTCTAATAAATTT. We suggest that, unlike other phage operators, the P1 repressor binding sites lack rotational symmetry.

MeSH Terms
Base Sequence Binding Sites Cloning, Molecular Coliphages/metabolism DNA, Viral Molecular Sequence Data Plasmids Repressor Proteins/metabolism Transcription Factors/metabolism Viral Proteins/metabolism
Chemicals
DNA, Viral Repressor Proteins Transcription Factors Viral Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Eliason J L
Central Research and Development Department, E. I. du Pont de Nemours and Company, Inc., Wilmington, DE 19898.
Sternberg N
Article Info
Journal
Journal of molecular biology
Abbr.
J Mol Biol
ISSN
0022-2836
Published
1987-11-20
Pages
281-93
Language
English
Region
England
NLM ID
2985088R
Subset
IM
Databases
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