Abstract
Genetic recombination in Escherichia coli is stimulated by the recombination hotspot Chi (χ), a regulatory element that modifies the activities of the RecBCD enzyme and leads to loading of the DNA strand exchange protein, RecA, onto the χ-containing DNA strand. The RecBC enzyme, which lacks the RecD subunit, loads RecA protein constitutively, in a manner that is independent of χ. Using a truncated RecBC enzyme lacking the 30 kDa C-terminal domain of the RecB subunit, we show that this domain is necessary for RecA protein-loading. We propose that this domain harbors a site that interacts with RecA protein, recruiting it to single-stranded DNA during unwinding. This ability of a translocating enzyme to deliver material (RecA protein) to a specific target site (the χ sequence) parallels that of other cellular motor proteins. (C) 2000 Academic Press.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 537-542 |
| Number of pages | 6 |
| Journal | Journal of Molecular Biology |
| Volume | 297 |
| Issue number | 3 |
| DOIs | |
| State | Published - Mar 31 2000 |
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Keywords
- Chi sequence
- Helicase
- RecA protein
- RecBCD enzyme
- Recombination
ASJC Scopus subject areas
- Virology
Cite this
Identification of the RecA protein-loading domain of RecBCD enzyme. / Churchill, Jason J.; Kowalczykowski, Stephen C.
In: Journal of Molecular Biology, Vol. 297, No. 3, 31.03.2000, p. 537-542.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Identification of the RecA protein-loading domain of RecBCD enzyme
AU - Churchill, Jason J.
AU - Kowalczykowski, Stephen C.
PY - 2000/3/31
Y1 - 2000/3/31
N2 - Genetic recombination in Escherichia coli is stimulated by the recombination hotspot Chi (χ), a regulatory element that modifies the activities of the RecBCD enzyme and leads to loading of the DNA strand exchange protein, RecA, onto the χ-containing DNA strand. The RecBC enzyme, which lacks the RecD subunit, loads RecA protein constitutively, in a manner that is independent of χ. Using a truncated RecBC enzyme lacking the 30 kDa C-terminal domain of the RecB subunit, we show that this domain is necessary for RecA protein-loading. We propose that this domain harbors a site that interacts with RecA protein, recruiting it to single-stranded DNA during unwinding. This ability of a translocating enzyme to deliver material (RecA protein) to a specific target site (the χ sequence) parallels that of other cellular motor proteins. (C) 2000 Academic Press.
AB - Genetic recombination in Escherichia coli is stimulated by the recombination hotspot Chi (χ), a regulatory element that modifies the activities of the RecBCD enzyme and leads to loading of the DNA strand exchange protein, RecA, onto the χ-containing DNA strand. The RecBC enzyme, which lacks the RecD subunit, loads RecA protein constitutively, in a manner that is independent of χ. Using a truncated RecBC enzyme lacking the 30 kDa C-terminal domain of the RecB subunit, we show that this domain is necessary for RecA protein-loading. We propose that this domain harbors a site that interacts with RecA protein, recruiting it to single-stranded DNA during unwinding. This ability of a translocating enzyme to deliver material (RecA protein) to a specific target site (the χ sequence) parallels that of other cellular motor proteins. (C) 2000 Academic Press.
KW - Chi sequence
KW - Helicase
KW - RecA protein
KW - RecBCD enzyme
KW - Recombination
UR - http://www.scopus.com/inward/record.url?scp=0034737310&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034737310&partnerID=8YFLogxK
U2 - 10.1006/jmbi.2000.3590
DO - 10.1006/jmbi.2000.3590
M3 - Article
C2 - 10731409
AN - SCOPUS:0034737310
VL - 297
SP - 537
EP - 542
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 3
ER -