Kowalczykowski Lab - UC Davis
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Interaction of Escherichia coli RecA protein with LexA repressor. I. LexA repressor cleavage is competitive with binding...

Rehrauer, Wm Lavery, Pe Palmer, El Singh, Rn Stephen Charles Kowalczykowski

Published in Journal of Biological Chemistry

Essential to the two distinct cellular events of genetic recombination and SOS induction in Escherichia coli, RecA protein promotes the homologous pairing and exchange of DNA strands and the proteolytic cleavage of the LexA repressor, respectively. Since both of these activities require single-stranded DNA (ssDNA) and ATP, the inter-relationship be...

Biochemical characterization of a mutant RecA protein altered in DNA-binding loop 1.

Mirshad, Jk Stephen Charles Kowalczykowski

Published in Biochemistry

The double substitution of Glu156 with Leu and Gly157 with Val in the Escherichia coli RecA protein results in a severely reduced level of recombination and constitutive coprotease behavior. Here we present our examination of the biochemical properties of this mutant protein, RecA N99, in an effort to understand its phenotype and the role of loop 1...

Rad52 protein associates with replication protein A (RPA)-single-stranded DNA to accelerate Rad51-mediated displacement ...

Sugiyama, T Stephen Charles Kowalczykowski

Published in Journal of Biological Chemistry

The Rad51 nucleoprotein filament mediates DNA strand exchange, a key step of homologous recombination. This activity is stimulated by replication protein A (RPA), but only when RPA is introduced after Rad51 nucleoprotein filament formation. In contrast, RPA inhibits Rad51 nucleoprotein complex formation by prior binding to single-stranded DNA (ssDN...

Biochemical basis of the constitutive coprotease activity of RecA P67W protein.

Mirshad, Jk Stephen Charles Kowalczykowski

Published in Biochemistry

The mutation of Pro67 to Trp (P67W) in the Escherichia coli RecA protein results in reduced recombination and constitutive coprotease phenotypes. We examined the biochemical properties of this mutant in an effort to understand these altered behaviors. We find that RecA P67W protein can access single-stranded DNA (ssDNA) binding sites within regions...

DNA annealing mediated by Rad52 and Rad59 proteins.

Wu, Y Sugiyama, T Stephen Charles Kowalczykowski

Published in Journal of Biological Chemistry

In the budding yeast Saccharomyces cerevisiae, the RAD52 gene is essential for all homologous recombination events and its homologue, the RAD59 gene, is important for those that occur independently of RAD51. Both Rad52 and Rad59 proteins can anneal complementary single-stranded (ss) DNA. We quantitatively examined the ssDNA annealing activity of Ra...

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 and topoisomerase III comprise a novel DNA strand passage function: a conserved mechanism for control of D...

Harmon, Fg Digate, Rj Stephen Charles Kowalczykowski

Published in Molecular Cell

E. coli RecQ protein is a multifunctional helicase with homologs that include the S. cerevisiae Sgs1 helicase and the H. sapiens Wrn and Blm helicases. Here we show that RecQ helicase unwinds a covalently closed double-stranded DNA (dsDNA) substrate and that this activity specifically stimulates E. coli topoisomerase III (Topo III) to fully catenat...

Alteration of χ recognition by RecBCD reveals a regulated molecular latch and suggests a channel-bypass mechanism for bi...

Yang, L Naofumi Handa Liu, B Dillingham, Ms Wigley, Db Stephen Charles Kowalczykowski

Published in Proceedings of the National Academy of Sciences

The RecBCD enzyme is a complex heterotrimeric helicase/nuclease that initiates recombination at double-stranded DNA breaks. In Escherichia coli, its activities are regulated by the octameric recombination hotspot, χ (5 -GCTGGTGG), which is read as a single-stranded DNA sequence while the enzyme is unwinding DNA at over ∼1,000 bp/s. Previous studies...

Cooperative and noncooperative binding of protein ligands to nucleic acid lattices: experimental approaches to the deter...

Stephen Charles Kowalczykowski Paul, Ls Lonberg, N Newport, Jw Mcswiggen, Ja Von Hippel, Ph

Published in Biochemistry

Many biologically important proteins bind nonspecifically, and often cooperatively, to single-or double-stranded nucleic acid lattices in discharging their physiological functions. This binding can generally be described in thermodynamic terms by three parameters: n, the binding site size; K, the intrinsic binding constant; omega, the binding coope...

Some assembly required.

Stephen Charles Kowalczykowski

Published in Nautre Structural Biology

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