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Specific activation of open complex formation at an Escherichia coli promoter by oligo(N-methylpyrrolecarboxamide)s: effects of peptide length and identification of DNA target sites

Martello, Pamela A. and Bruzik, James P. and deHaseth, Pieter and Youngquist, R. Scott and Dervan, Peter B. (1989) Specific activation of open complex formation at an Escherichia coli promoter by oligo(N-methylpyrrolecarboxamide)s: effects of peptide length and identification of DNA target sites. Biochemistry, 28 (10). pp. 4455-61. ISSN 0006-2960. http://resolver.caltech.edu/CaltechAUTHORS:20160511-144146309

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Abstract

It has previously been shown that open complex formation at a promoter containing a block substitution of nonalternating A-T sequences in the spacer DNA separating the contacted -10 and -35 regions could be accelerated by distamycin. No stimulation was observed at a promoter with a substitution of alternating A-T base pairs in the same region or at the promoter with wild-type spacer. Here we compare the effect of distamycin [tris(N-methylpyrrolecarboxamide), formally a P3] with that of its extended homologues P4, P5, and P6. It is found that the stimulatory potential of these synthetic oligopeptides which bind in the minor groove of DNA ranks in the order P4 greater than (distamycin, P5) greater than P6. The interaction of these peptides with the three promoters was studied by monitoring the positions of the promoter DNA protected from MPE-Fe(II) cleavage in the presence of different concentrations of ligand. The results suggest that a higher affinity of oligopeptide for the spacer DNA than for the -10 and/or -35 region is a necessary, but not sufficient condition for stimulation. Different patterns of protected DNA regions are seen with each of the three promoters; with distamycin, P4, and P5, a unique arrangement of protected regions is observed for the variant containing nonalternating A-T base pairs in its spacer DNA. These data support the hypothesis that differences in the ways the minor-groove binders interact with each of the promoter variants account for the observed differential stimulation. We further postulate that it is a ligand-induced structural change in the nonalternating A-T DNA which is responsible for the activation of open complex formation at the promoter containing this substitution.


Item Type:Article
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URLURL TypeDescription
http://dx.doi.org/10.1021/bi00436a050DOIArticle
http://pubs.acs.org/doi/abs/10.1021/bi00436a050PublisherArticle
Additional Information:© 1989 American Chemical Society. Received November 21, 1988. Revised Manuscript Received February 1, 1989. P.B.D. and P.d.H. are grateful to the National Institutes of Health for research support (GM-27681 and GM-31808, respectively). We appreciate the careful review of the manuscript by the referees.
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Funding AgencyGrant Number
NIHGM-27681
NIHGM-31808
Record Number:CaltechAUTHORS:20160511-144146309
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20160511-144146309
Official Citation:Specific activation of open complex formation at an Escherichia coli promoter by oligo(N-methylpyrrolecarboxamide)s: effects of peptide length and identification of DNA target sites Pamela A. Martello, James P. Bruzik, Pieter DeHaseth, R. Scott Youngquist, and Peter B. Dervan Biochemistry 1989 28 (10), 4455-4461 DOI: 10.1021/bi00436a050
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:67009
Collection:CaltechAUTHORS
Deposited By: Victoria Brennan
Deposited On:19 May 2016 22:48
Last Modified:19 May 2016 22:48

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