Abstracts - faqs.org

Abstracts

Biological sciences

Search abstracts:
Abstracts » Biological sciences

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

Article Abstract:

A novel pairing process has been found to be promoted by Escherichia coli RecA protein and to involve inverse RNA and DNA strand swapping. RecA protein polymerizes along dsDNA forming an active nucleoprotien filament that can hook up and exchange strands with homologous ssDNA. The reaction in reverse is very efficient. It does not come from redistribution of ReA protein from dsDNA to the homologous ssDNA. The recA protein-dsDNA filament can hook up and promote strand exchange with ssRNA as well. Likely the inverse RNA strand exchange reaction is responsible for R-loop formation needed for recombination-dependent DNA replication.

Author: Zaitsev, Eugene N., Kowalczykowski, Stephen C.
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 2000
Carrier proteins, Transport proteins, Escherichia coli, Recombinant DNA, Cytochemistry, RNA splicing

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


The RecBC enzyme loads RecA protein onto ssDNA asymmetrically and independently of x, resulting in constitutive recombination activation

Article Abstract:

Studies indicate that constitutive recombination activity is prompted by RecA protein loading, which is a RecBCD holoenzyme latent property. Normally, RecA is blocked by the subunit RecD and is only revealed following interaction with cis-acting elements, or x sites. However, the RecBC enzyme, without RecD, loads RecA protein onto the DNA strand constitutively.

Author: Kowalczykowski, Stephen C., Anderson, Daniel G., Churchill, Jason J.
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 1999
Enzymes, Proteins, Enzyme regulation

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


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

Article Abstract:

Activation of double-stranded DNA (dsDNA) for strand exchange, a novel property of the RecA nucleoprotein filament, is discussed. The novel DNA strand exchange is referred to as being in trans (ital) and the RecA nucleoprotein filament is a protein scaffold activating dsDNA for strange exchange with singe-stranded DNA (ssDNA) within or outside the filament.

Author: Kowalczykowski, Stephen C., Mazin, Alexander V.
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 1999
Statistical Data Included, DNA, Physiological regulation, Protein binding, Homology (Biology), Biological control systems

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Subjects list: Research, United States, Genetic aspects, Genetic recombination
Similar abstracts:
  • Abstracts: The Desulfuromonas acetoxidans triheme cytochrome c7 produced in Desulfovibrio desulfuricans retains its metal reductase activity
  • Abstracts: The zinc ribbon domains of the general transcription factors TFIIB and Brf: conserved functional surfaces but different roles in transcription initiation
  • Abstracts: The carboxyl terminus of phage HK022 Nun includes a novel zinc-binding motif and a tryptophan required for transcription termination
This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.
Some parts © 2025 Advameg, Inc.