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) |
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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 |
Keywords
- Chi sequence
- Helicase
- RecA protein
- RecBCD enzyme
- Recombination
ASJC Scopus subject areas
- Virology