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Journal of Bacteriology, June 2004, p. 3599-3608, Vol. 186, No. 11
0021-9193/04/$08.00+0 DOI: 10.1128/JB.186.11.3599-3608.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
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Department of Molecular Biology and Genetics, Cornell University Ithaca, New York 14853
Received 3 December 2003/ Accepted 16 February 2004
Bacteriophage
gene Q protein and the related proteins of other lambdoid phages are transcription antiterminators that interact both with DNA in the late gene promoter segment and with RNA polymerase subunits. Using hybrids between Q of
and the related Q of phage 80, we characterized elements of both Q and DNA that contribute to the DNA binding function. In particular, we found a C-terminal segment of the protein that is responsible for binding specificity and an
15 residue segment on a predicted alpha helix within this segment at which alanine substitutions decrease DNA binding. We identified a six-nucleotide segment located between the 35 and 10 promoter elements that confers binding specificity and is the site of point mutants that impair binding, and we isolated suppressors in
Q that restore binding function by increasing the overall binding affinity. We also identified putative zinc finger structures in both proteins.
Present address: Department of Genetics and Genomics, Roche Palo Alto, Palo Alto, CA 94304.
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