Structural motif of the DNA binding domain of γδ-resolvase characterized by affinity cleaving
- Creators
- Graham, Kenneth S.
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Dervan, Peter B.
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.
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.).Attached Files
Published - J._Biol._Chem.-1990-Graham-16534-40.pdf
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Additional details
- Eprint ID
- 66963
- Resolver ID
- CaltechAUTHORS:20160510-155631020
- Defense Advanced Research Projects Agency (DARPA)
- NIH Predoctoral Fellowship
- Created
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2016-05-18Created from EPrint's datestamp field
- Updated
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2019-11-26Created from EPrint's last_modified field