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

Jason J. Churchill, Daniel G. Anderson, Stephen C. Kowalczykowski

Research output: Contribution to journalArticle

97 Citations (Scopus)

Abstract

Double-strand DNA break repair and homologous recombination in Escherichia coil proceed by the RecBCD pathway, which is regulated by cis- acting elements known as χ sites. A crucial feature of this regulation is the RecBCD enzyme-directed loading of RecA protein specifically onto the 3'- terminal, χ-containing DNA strand. Here we show that RecBC enzyme (lacking the RecD subunit) loads RecA protein constitutively onto the 3'-terminal DNA strand, with no requirement for χ. This strand is preferentially utilized in homologous pairing reactions. We propose that RecA protein loading is a latent property of the RecBCD holoenzyme, which is normally blocked by the RecD subunit and is revealed following interaction with χ.

Original languageEnglish (US)
Pages (from-to)901-911
Number of pages11
JournalGenes and Development
Volume13
Issue number7
StatePublished - Apr 1 1999

Fingerprint

Rec A Recombinases
Genetic Recombination
Exodeoxyribonuclease V
Enzymes
Escherichia
Holoenzymes
Double-Stranded DNA Breaks
Homologous Recombination
DNA
DNA Repair

Keywords

  • χ
  • DNA repair
  • Helicase
  • RecA
  • RecBC
  • Recombination

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

Cite this

The RecBC enzyme loads recA protein onto ssDNA asymmetrically and independently of χ, resulting in constitutive recombination activation. / Churchill, Jason J.; Anderson, Daniel G.; Kowalczykowski, Stephen C.

In: Genes and Development, Vol. 13, No. 7, 01.04.1999, p. 901-911.

Research output: Contribution to journalArticle

Churchill, Jason J. ; Anderson, Daniel G. ; Kowalczykowski, Stephen C. / The RecBC enzyme loads recA protein onto ssDNA asymmetrically and independently of χ, resulting in constitutive recombination activation. In: Genes and Development. 1999 ; Vol. 13, No. 7. pp. 901-911.
@article{21147873049949f290b527966bb4196b,
title = "The RecBC enzyme loads recA protein onto ssDNA asymmetrically and independently of χ, resulting in constitutive recombination activation",
abstract = "Double-strand DNA break repair and homologous recombination in Escherichia coil proceed by the RecBCD pathway, which is regulated by cis- acting elements known as χ sites. A crucial feature of this regulation is the RecBCD enzyme-directed loading of RecA protein specifically onto the 3'- terminal, χ-containing DNA strand. Here we show that RecBC enzyme (lacking the RecD subunit) loads RecA protein constitutively onto the 3'-terminal DNA strand, with no requirement for χ. This strand is preferentially utilized in homologous pairing reactions. We propose that RecA protein loading is a latent property of the RecBCD holoenzyme, which is normally blocked by the RecD subunit and is revealed following interaction with χ.",
keywords = "χ, DNA repair, Helicase, RecA, RecBC, Recombination",
author = "Churchill, {Jason J.} and Anderson, {Daniel G.} and Kowalczykowski, {Stephen C.}",
year = "1999",
month = "4",
day = "1",
language = "English (US)",
volume = "13",
pages = "901--911",
journal = "Genes and Development",
issn = "0890-9369",
publisher = "Cold Spring Harbor Laboratory Press",
number = "7",

}

TY - JOUR

T1 - The RecBC enzyme loads recA protein onto ssDNA asymmetrically and independently of χ, resulting in constitutive recombination activation

AU - Churchill, Jason J.

AU - Anderson, Daniel G.

AU - Kowalczykowski, Stephen C.

PY - 1999/4/1

Y1 - 1999/4/1

N2 - Double-strand DNA break repair and homologous recombination in Escherichia coil proceed by the RecBCD pathway, which is regulated by cis- acting elements known as χ sites. A crucial feature of this regulation is the RecBCD enzyme-directed loading of RecA protein specifically onto the 3'- terminal, χ-containing DNA strand. Here we show that RecBC enzyme (lacking the RecD subunit) loads RecA protein constitutively onto the 3'-terminal DNA strand, with no requirement for χ. This strand is preferentially utilized in homologous pairing reactions. We propose that RecA protein loading is a latent property of the RecBCD holoenzyme, which is normally blocked by the RecD subunit and is revealed following interaction with χ.

AB - Double-strand DNA break repair and homologous recombination in Escherichia coil proceed by the RecBCD pathway, which is regulated by cis- acting elements known as χ sites. A crucial feature of this regulation is the RecBCD enzyme-directed loading of RecA protein specifically onto the 3'- terminal, χ-containing DNA strand. Here we show that RecBC enzyme (lacking the RecD subunit) loads RecA protein constitutively onto the 3'-terminal DNA strand, with no requirement for χ. This strand is preferentially utilized in homologous pairing reactions. We propose that RecA protein loading is a latent property of the RecBCD holoenzyme, which is normally blocked by the RecD subunit and is revealed following interaction with χ.

KW - χ

KW - DNA repair

KW - Helicase

KW - RecA

KW - RecBC

KW - Recombination

UR - http://www.scopus.com/inward/record.url?scp=0033119260&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033119260&partnerID=8YFLogxK

M3 - Article

C2 - 10197989

AN - SCOPUS:0033119260

VL - 13

SP - 901

EP - 911

JO - Genes and Development

JF - Genes and Development

SN - 0890-9369

IS - 7

ER -