The mechanism of loading of the FLP recombinase onto its DNA target sequence.

Abstract:

:The FLP recombinase interacts with its target sequence with the formation of three distinct DNA-protein complexes. The first complex leaves neither a DNase footprint nor is the DNA protected from methylation by dimethyl sulfate. We have found, however, that the FLP protein is bound predominantly to only one of the three 13 base-pair (bp) symmetry elements. This asymmetric loading of the FLP site seems to require the presence of an adjacent directly repeated 13 bp element. We speculate that this asymmetric filling of the target site may be accompanied by the unique order of cleavage and exchange of DNA strands.

journal_name

J Mol Biol

authors

Beatty LG,Sadowski PD

doi

10.1016/0022-2836(88)90576-1

subject

Has Abstract

pub_date

1988-11-20 00:00:00

pages

283-94

issue

2

eissn

0022-2836

issn

1089-8638

pii

0022-2836(88)90576-1

journal_volume

204

pub_type

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