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The RecBC enzyme loads RecA protein onto ssDNA asymmetrically and independently of chi, resulting in constitutive recomb...

Churchill, Jj Anderson, Dg Stephen Charles Kowalczykowski

Published in Genes & Development

Double-strand DNA break repair and homologous recombination in Escherichia coli proceed by the RecBCD pathway, which is regulated by cis-acting elements known as chi sites. A crucial feature of this regulation is the RecBCD enzyme-directed loading of RecA protein specifically onto the 3 -terminal, chi-containing DNA strand. Here we show that RecBC ...

RecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination.

Harmon, Fg Stephen Charles Kowalczykowski

Published in Genes & Development

RecQ helicase is important to homologous recombination and DNA repair in Escherichia coli. We demonstrate that RecQ helicase, in conjunction with RecA and SSB proteins, can initiate recombination events in vitro. In addition, RecQ protein is capable of unwinding a wide variety of DNA substrates, including joint molecules formed by RecA protein. The...

BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end resection machineries for human DNA break repair.

Nimonkar, Amitabh V Genschel, Jochen Kinoshita, Eri Polaczek, Piotr Campbell, Judith L Wyman, Claire Modrich, Paul Kowalczykowski, Stephen C

Published in Genes & development

Repair of dsDNA breaks requires processing to produce 3'-terminated ssDNA. We biochemically reconstituted DNA end resection using purified human proteins: Bloom helicase (BLM); DNA2 helicase/nuclease; Exonuclease 1 (EXO1); the complex comprising MRE11, RAD50, and NBS1 (MRN); and Replication protein A (RPA). Resection occurs via two routes. In one, ...

The recombination hot spot chi is a regulatory element that switches the polarity of DNA degradation by the RecBCD enzym...

Anderson, Dg Stephen Charles Kowalczykowski

Published in Genes & Development

Homologous recombination in Escherichia coli is stimulated at DNA sequences known as chi sites. Stimulation requires the multifunctional RecBCD enzyme, which is both a helicase and a 3 —> 5 exonuclease. Upon recognition of a properly oriented chi site, the 3 —> 5 exonuclease activity is attenuated. Here we show that in addition to attenuation o...

A novel property of the RecA nucleoprotein filament: activation of double- stranded DNA for strand exchange in trans.

Mazin, Av Stephen Charles Kowalczykowski

Published in Genes & Development

RecA protein catalyzes DNA strand exchange, a basic step of homologous recombination. Upon binding to single-stranded DNA (ssDNA), RecA protein forms a helical nucleoprotein filament. Normally, this nucleoprotein filament binds double-stranded DNA (dsDNA) and promotes exchange of base pairs between this dsDNA and the homologous ssDNA that is contai...

A novel pairing process promoted by Escherichia coli RecA protein: inverse DNA and RNA strand exchange.

Zaitsev, En Stephen Charles Kowalczykowski

Published in Genes & Development

Traditionally, recombination reactions promoted by RecA-like proteins initiate by forming a nucleoprotein filament on a single-stranded DNA (ssDNA), which then pairs with homologous double-stranded DNA (dsDNA). In this paper, we describe a novel pairing process that occurs in an unconventional manner: RecA protein polymerizes along dsDNA to form an...

In vitro selection of preferred DNA pairing sequences by the Escherichia coli RecA protein.

Tracy, Rb Stephen Charles Kowalczykowski

Published in Genes & Development

The RecA protein and other DNA strand exchange proteins are characterized by their ability to bind and pair DNA in a sequence-independent manner. In vitro selection experiments demonstrate, unexpectedly, that RecA protein has a preferential affinity for DNA sequences rich in GT composition. Such GT-rich sequences are present in loci that display in...

RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange.

Seitz, Em Brockman, Jp Sandler, Sj Clark, Aj Stephen Charles Kowalczykowski

Published in Genes & Development

With the discovery that the Saccharomyces cerevisiae Rad51 protein is both structurally and functionally similar to the Escherichia coli RecA protein, the RecA paradigm for homologous recombination was extended to the Eucarya. The ubiquitous presence of RecA and Rad51 protein homologs raises the question of whether this archetypal protein exists wi...

The preference for GT-rich DNA by the yeast Rad51 protein defines a set of universal pairing sequences.

Tracy, Rb Baumohl, Jk Stephen Charles Kowalczykowski

Published in Genes & Development

The Rad51 protein of Saccharomyces cerevisiae is a eukaryotic homolog of the RecA protein, the prototypic DNA strand-exchange protein of Escherichia coli. RAD51 gene function is required for efficient genetic recombination and for DNA double-strand break repair. Recently, we demonstrated that RecA protein has a preferential affinity for GT-rich DNA...

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