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Structural motif of the DNA binding domain of γδ-resolvase characterized by affinity cleaving

Graham, Kenneth S. and Dervan, Peter B. (1990) Structural motif of the DNA binding domain of γδ-resolvase characterized by affinity cleaving. Journal of Biological Chemistry, 265 (27). pp. 16534-16540. ISSN 0021-9258. https://resolver.caltech.edu/CaltechAUTHORS:20160510-155631020

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Abstract

The DNA binding domain of γδ-resolvase, residues 141-183, is thought to bind DNA by a helix-turn-helix motif based on sequence similarities with other known DNA binding proteins. Incorporation of the DNA cleaving moiety, EDTA Fe, at the NH2 and COOH termini of γδ(141-183) allows the positions of these residues relative to the DNA bases at three resolvase binding sites, each consisting of inverted copies of an imperfectly conserved 9-base pair sequence, to be mapped by high resolution gel electrophoresis. The cleavage data for EDTA-γδ(141-183) reveals that the NH2 terminus of the DNA binding domain of gamma delta-resolvase is bound proximal to the minor groove of DNA near the center of the resolvase binding sites. Cleavage by EDTA Fe attached to a lysine side chain (Asn^(183)→Lys^(183)) at the COOH terminus of γδ(141-183) reveals that the putative recognition helix is in the adjacent major groove on the same face of the helix, oriented toward the center of the inverted repeats.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://www.jbc.org/content/265/27/16534.abstractPublisherArticle
ORCID:
AuthorORCID
Dervan, Peter B.0000-0001-8852-7306
Additional Information:© 1990 The American Society for Biochemistry and Molecular Biology, Inc. Received for publication, March 1, 1990. This work was supported in part by the DARPA University Research Initiative Program and by a National Research Service Award from the National Institute of General Medical Sciences (to K. S. G.).
Funders:
Funding AgencyGrant Number
Defense Advanced Research Projects Agency (DARPA)UNSPECIFIED
NIH Predoctoral FellowshipUNSPECIFIED
Issue or Number:27
Record Number:CaltechAUTHORS:20160510-155631020
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20160510-155631020
Official Citation:K S Graham and P B Dervan Structural motif of the DNA binding domain of gamma delta-resolvase characterized by affinity cleaving. J. Biol. Chem. 1990 265: 16534-40.
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:66963
Collection:CaltechAUTHORS
Deposited By: Victoria Brennan
Deposited On:18 May 2016 23:57
Last Modified:26 Nov 2019 11:15

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