Domain of a yeast site-specific recombinase (Flp) that recognizes its target site
Abstract
Binding of a partial proteolytic digest by V8 enzyme of the yeast site-specific recombinase Flp to its target site gives rise to DNA-protein complexes that are smaller than those produced by the full-sized protein. The smallest of these complexes (occupancy of one peptide monomer per site) contains either one of two polypeptides (32 and 28 kDa) of the V8 digestion mixture. The amino termini of both polypeptides map to Ser-129 of Flp, corresponding to V8 cleavage at Glu-128. The relative mobilities of the complexes formed by the V8 peptides indicate that they lack the sharp substrate bend that is characteristic of Flp-derived complexes. A hybrid protein consisting of the amino-terminal one-third of the R recombinase (from Zygosaccharomyces rouxii) and the carboxyl-terminal two-thirds of Flp recognizes the Flp target site.
Additional Information
© 2014 National Academy of Sciences. Communicated by Esmond E. Snell, April 1, 1991. We acknowledge the gift of the R recombinase expression plasmid from H. Araki and Y. Oshima. We thank Lei Zheng, Christine Acklin, and Tammy Bauer for excellent technical assistance. This work was supported by National Institutes of Health funds to M.J. and by National Science Foundation Grant DIR 86-18937 to D.B.T.Attached Files
Published - PNAS-1991-Chen-5944-8.pdf
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Additional details
- PMCID
- PMC51998
- Eprint ID
- 53101
- Resolver ID
- CaltechAUTHORS:20141222-131437336
- NIH
- DIR 86-18937
- NSF
- Created
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2014-12-22Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field