• Documents
  • Authors
  • Tables
  • Log in
  • Sign up
  • MetaCart
  • DMCA
  • Donate

CiteSeerX logo

Advanced Search Include Citations
Advanced Search Include Citations

A single mutation, RecB(D1080A), eliminates RecA protein loading but not Chi recognition by RecBCD enzyme (1999)

by Daniel G. Anderson, Jason J. Churchill, Stephen C. Kowalczykowski
Add To MetaCart

Tools

Sorted by:
Results 1 - 8 of 8

RecBCD enzyme and the repair of double-stranded DNA breaks

by Mark S. Dillingham, Stephen C. Kowalczykowski, Mark S. Dillingham, Stephen C. Kowalczykowski - Microbiol. Mol. Rev , 2008
"... Updated information and services can be found at: ..."
Abstract - Cited by 29 (4 self) - Add to MetaCart
Updated information and services can be found at:
(Show Context)

Citation Context

...to interact directly with the RecA protein (67, 270). This interaction plays an essential role in the mechanism of loading the RecA protein onto the Chi-containing ssDNA produced by the RecBCD enzyme =-=(13, 17, 23)-=-. Modeling of the interaction between RecA and the nuclease domain of RecB suggests that it is similar to the RecA-RecA interface in the nucleoprotein filament (270). Consequently, it was suggested th...

A comparison of responses to double-strand breaks between Escherichia coli and Bacillus subtilis reveals different requirements for SOS induction

by Lyle A. Simmons, Alexi I. Goranov, Hajime Kobayashi, Bryan W. Davies, Daniel S. Yuan, Alan D. Grossman, Graham C. Walker, Lyle A. Simmons, Alexi I. Goranov, Hajime Kobayashi, Bryan W. Davies, Daniel S. Yuan, Alan D. Grossman, Graham C. Walker - J. Bacteriol , 2008
"... These include: This article cites 84 articles, 36 of which can be accessed free at: ..."
Abstract - Cited by 6 (1 self) - Add to MetaCart
These include: This article cites 84 articles, 36 of which can be accessed free at:

In vivo evidence for two active nuclease motifs in the double–strand break repair enzyme RexAB of Lactococcus lactis

by Andréa Quiberoni, Indranil Biswas, Meriem El Karoui, Patrick Tailliez, Ra Gruss, J. Bacteriol, Of Lactococcus Lactis, Andréa Quiberoni, Indranil Biswas, Meriem El Karoui, Lahcen Rezaïki, Patrick Tailliez, Alexandra Gruss - J. Bacteriol , 2001
"... Updated information and services can be found at: ..."
Abstract - Cited by 3 (0 self) - Add to MetaCart
Updated information and services can be found at:
(Show Context)

Citation Context

... maintains RecBCD incompetent for homologous recombination prior to Chi; at Chi, RecD is suggested to undergo a conformational change that attenuates exonuclease activity and stimulates recombination =-=(2, 3, 12, 33, 48)-=-. A swing model was proposed in which RecD assures proximity of the RecB nuclease with both DNA strands prior to Chi and a repositioning of the nuclease after Chi (51, 54). Organization of the two-sub...

Genetic Requirements for High Constitutive SOS Expression in recA730 Mutants of Escherichia coli

by unknown authors , 2011
"... The RecA protein in its functional state is in complex with single-stranded DNA, i.e., in the form of a RecA filament. In SOS induction, the RecA filament functions as a coprotease, enabling the autodigestion of the LexA repressor. The RecA filament can be formed by different mechanisms, but all of ..."
Abstract - Add to MetaCart
The RecA protein in its functional state is in complex with single-stranded DNA, i.e., in the form of a RecA filament. In SOS induction, the RecA filament functions as a coprotease, enabling the autodigestion of the LexA repressor. The RecA filament can be formed by different mechanisms, but all of them require three enzymatic activities essential for the processing of DNA double-stranded ends. These are helicase, 5–3 exonuclease, and RecA loading onto single-stranded DNA (ssDNA). In some mutants, the SOS response can be expressed constitutively during the process of normal DNA metabolism. The RecA730 mutant protein is able to form the RecA filament without the help of RecBCD and RecFOR mediators since it better competes with the single-strand binding (SSB) protein for ssDNA. As a consequence, the recA730 mutants show high constitutive SOS expression. In the study described in this paper, we studied the genetic requirements for constitutive SOS expression in recA730 mutants. Using a -galactosidase assay, we showed that the constitutive SOS response in recA730 mutants exhibits different requirements in different backgrounds. In a wild-type background, the constitutive SOS response is partially dependent on RecBCD function. In a recB1080 background (the recB1080 mutation retains only helicase), constitutive SOS expression is partially dependent on RecBCD helicase function and is strongly dependent on RecJ nuclease. Finally, in a recB-null background, the constitutive SOS expression of the recA730 mutant is
(Show Context)

Citation Context

...RecFOR. There is a specific mutation in the recB nuclease center (i.e., recB1080) which partially affects the RecBCD function, preserving helicase but eliminating nuclease and RecA loading activities =-=(2, 41, 45)-=-. In a recB1080 mutant, the components of the two recombination machineries (RecBCD and RecF) are interchangeable and the processing of DSBs is dependent on RecB1080CD (helicase), RecJ (5–3 exonucle...

Genetic Evidence for the Requirement of RecA Loading Activity in SOS Induction after UV Irradiation in Escherichia coli

by Krunoslav Brcic-kostic, Ivana Ivancic-bace, Ignacija Vlasic, Erika Salaj-smic , 2006
"... This article cites 37 articles, 11 of which can be accessed free ..."
Abstract - Add to MetaCart
This article cites 37 articles, 11 of which can be accessed free
(Show Context)

Citation Context

... also involved in RecA binding (33). Consequently, the RecB1080CD form of the enzyme is nuclease deficient and is unable to load RecA protein onto ssDNA, but it still has functional helicase activity =-=(2, 37, 40)-=-. In this study we compared the levels of SOS induction after UV irradiation in strains in which one or both mechanisms of RecA loading activity were inactivated. We found that RecA loading activity i...

COMMUNIC r

by unknown authors
"... on), a e a th cD pe erm ssa ite A m all nz such as conjugation, transductio double-stranded DNA (dsDNA either during DNA replication Michel et al., 1997) or as a resu (for a review, see Friedberg RecBCD enzyme consists of ..."
Abstract - Add to MetaCart
on), a e a th cD pe erm ssa ite A m all nz such as conjugation, transductio double-stranded DNA (dsDNA either during DNA replication Michel et al., 1997) or as a resu (for a review, see Friedberg RecBCD enzyme consists of
(Show Context)

Citation Context

...s to preservation of the w-containing strand downstream of the w sequence (Anderson & Kowalczykowski, 1997a).1998b). We demonstrated that this RecBD1080ACD enzyme is also unable to load RecA protein (=-=Anderson et al., 1999-=-). We were also able to establish that, even though this mutant enzyme does not produce w-specific fragments, it does retain an ability to recognize the w sequence. These results allowed us to conclud...

Effects of recJ, recQ, and recFOR Mutations on Recombination in Nuclease-Deficient recB recD Double Mutants of Escherichia coli

by Doublerecb Recdnuclease-deficient , 2004
"... Updated information and services can be found at: ..."
Abstract - Add to MetaCart
Updated information and services can be found at:
(Show Context)

Citation Context

...situated on the C-terminal portion of the RecB subunit. The consequence of this mutation is that the RecB1080CD enzyme loses its nuclease and RecA loading activities but retains its helicase activity =-=(8, 48, 50)-=-. However, the recB1080 mutant is recombination proficient. Genetic analysis has shown that a hybrid recombination machinery operates in this mutant during initiation of recombination: the RecB1080CD ...

unknown title

by unknown authors
"... This article was originally published in a journal published by Elsevier, and the attached copy is provided by Elsevier for the author’s benefit and for the benefit of the author’s institution, for non-commercial research and educational use including without limitation use in instruction at your in ..."
Abstract - Add to MetaCart
This article was originally published in a journal published by Elsevier, and the attached copy is provided by Elsevier for the author’s benefit and for the benefit of the author’s institution, for non-commercial research and educational use including without limitation use in instruction at your institution, sending it to specific colleagues that you know, and providing a copy to your institution’s administrator. All other uses, reproduction and distribution, including without limitation commercial reprints, selling or licensing copies or access, or posting on open internet sites, your personal or institution’s website or repository, are prohibited. For exceptions, permission may be sought for such use through Elsevier’s permissions site at:
Powered by: Apache Solr
  • About CiteSeerX
  • Submit and Index Documents
  • Privacy Policy
  • Help
  • Data
  • Source
  • Contact Us

Developed at and hosted by The College of Information Sciences and Technology

© 2007-2019 The Pennsylvania State University