Kowalczykowski Lab - UC Davis
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1 News 192 Publications 19 Members

Formation of heteroduplex DNA promoted by the combined activities of Escherichia coli recA and recBCD proteins.

Roman, Lj Stephen Charles Kowalczykowski

Published in Journal of Biological Chemistry

We have established an in vitro reaction in which heteroduplex DNA formation is dependent on the concerted actions of recA and recBCD proteins, the major components of the recBCD pathway of genetic recombination in vivo. We find that heteroduplex DNA formation requires three distinct enzymatic functions: first, the helicase activity of recBCD enzym...

Transfer of recA protein from one polynucleotide to another. Kinetic evidence for a ternary intermediate during the tran...

Menetski, Jp Stephen Charles Kowalczykowski

Published in Journal of Biological Chemistry

We have analyzed the transfer kinetics of recA protein from one polynucleotide to another by monitoring the change in fluorescence of a modified single-stranded M13 DNA, referred to as etheno M13 DNA, that accompanies recA protein dissociation. The observed rate of transfer is dependent on the concentration of competitor polynucleotide, polythymidy...

Second-end DNA capture in double-strand break repair: how to catch a DNA by its tail.

Nimonkar, Av Stephen Charles Kowalczykowski

Published in Cell Cycle

Effects of the Escherichia coli SSB protein on the binding of Escherichia coli RecA protein to single-stranded DNA. Demo...

Stephen Charles Kowalczykowski Clow, J Somani, R Varghese, A

Published in Journal of Molecular Biology

The effect of the Escherichia coli single-stranded DNA binding (SSB) protein on the stability of complexes of E. coli RecA protein with single-stranded DNA has been investigated through direct DNA binding experiments. The effect of each protein on the binding of the other to single-stranded DNA, and the effect of SSB protein on the transfer rate of...

The simultaneous binding of two double-stranded DNA molecules by Escherichia coli RecA protein.

Zaitsev, En Stephen Charles Kowalczykowski

Published in Journal of Molecular Biology

We have characterized the double-stranded DNA (dsDNA) binding properties of RecA protein, using an assay based on changes in the fluorescence of 4 ,6-diamidino-2-phenylindole (DAPI)-dsDNA complexes. Here we use fluorescence, nitrocellulose filter-binding, and DNase I-sensitivity assays to demonstrate the binding of two duplex DNA molecules by the R...

RecA.

Galletto, R Stephen Charles Kowalczykowski

Published in Current Biology

Direct visualization of RecBCD movement reveals cotranslocation of the RecD motor after chi recognition.

Naofumi Handa Bianco, Pr Baskin, Rj Stephen Charles Kowalczykowski

Published in Molecular Cell

In Escherichia coli, chi (5 -GCTGGTGG-3 ) is a recombination hotspot recognized by the RecBCD enzyme. Recognition of chi reduces both nuclease activity and translocation speed of RecBCD and activates RecA-loading ability. RecBCD has two motor subunits, RecB and RecD, which act simultaneously but independently. A longstanding hypothesis to explain t...

Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. III. Binding properties of two specific prote...

Lonberg, N Stephen Charles Kowalczykowski Paul, Ls Von Hippel, Ph

Published in Journal of Molecular Biology

Enhanced monomer-monomer interactions can suppress the recombination deficiency of the recA142 allele.

Zaitsev, En Stephen Charles Kowalczykowski

Published in Molecular Microbiology

The RecA142 protein, in which valine is substituted for isoleucine-225, is defective for genetic recombination in vivo and for DNA strand exchange activity in vitro under conventional growth and reaction conditions respectively. However, we show that mildly acidic conditions restore both the in vitro DNA strand exchange activity and the in vivo fun...

Bipolar DNA translocation contributes to highly processive DNA unwinding by RecBCD enzyme.

Dillingham, Ms Webb, Mr Stephen Charles Kowalczykowski

Published in Journal of Biological Chemistry

We recently demonstrated that the RecBCD enzyme is a bipolar DNA helicase that employs two single-stranded DNA motors of opposite polarity to drive translocation and unwinding of duplex DNA. We hypothesized that this organization may explain the exceptionally high rate and processivity of DNA unwinding catalyzed by the RecBCD enzyme. Using a stoppe...

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