A study of the CopF repressor of plasmid pAMbeta1 by phage display.
We studied DNA binding of a transcriptional repressor, CopF, displayed on a filamentous phage. Mutagenesis of a putative helix-turn-helix motif of CopF and of certain bases of the operator abolished the protein-DNA interaction, establishing the elements involved in CopF function and showing that phage display can be used to study repressor proteins.
d'Alençon
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Génétique Microbienne, INRA, Domaine de Vilvert, 78352 Jouy en Josas Cedex, France.
Ehrlich
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D001426:Bacterial Proteins; D004269:DNA, Bacterial; D019077:Helix-Turn-Helix Motifs; D019151:Peptide Library; D010957:Plasmids; D012097:Repressor Proteins / Q000235:genetics* / Q000378:metabolism
D001426:Bacterial Proteins; C107074:CopF protein, bacteria; D004269:DNA, Bacterial; D019151:Peptide Library; D012097:Repressor Proteins