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 language | English (US) |
|---|---|
| Pages (from-to) | 901-911 |
| Number of pages | 11 |
| Journal | Genes and Development |
| Volume | 13 |
| Issue number | 7 |
| State | Published - Apr 1 1999 |
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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 journal › Article
}
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 -