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.

authors

Chen JW,Evans BR,Yang SH,Teplow DB,Jayaram M

doi

10.1073/pnas.88.14.5944

subject

Has Abstract

pub_date

1991-07-15 00:00:00

pages

5944-8

issue

14

eissn

0027-8424

issn

1091-6490

journal_volume

88

pub_type

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