Enzymatic formation and resolution of Holliday junctions in vitro.

Abstract:

:E. coli RecA protein promotes homologous pairing and reciprocal strand exchange reactions between duplex DNA molecules in vitro. Reaction intermediates contain Holliday junctions that are driven along the DNA at a maximal rate approaching 1000 bases per minute. T4 endonuclease VII cleaves Holliday junctions in vitro, and its inclusion in RecA-mediated reactions leads to the rapid formation of heteroduplex products. Product analysis indicates patch and splice recombinant molecules similar to those expected from in vivo recombination events. The combined formation and resolution of Holliday junctions has led us to propose a model for resolution based on the structure of RecA-DNA helices. One feature of this model is that resolution, which gives rise to the two types of recombinant product, may occur without need for isomerization of the junction.

journal_name

Cell

journal_title

Cell

authors

Müller B,Jones C,Kemper B,West SC

doi

10.1016/0092-8674(90)90747-3

subject

Has Abstract

pub_date

1990-01-26 00:00:00

pages

329-36

issue

2

eissn

0092-8674

issn

1097-4172

pii

0092-8674(90)90747-3

journal_volume

60

pub_type

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