Identification of the RecA protein-loading domain of RecBCD enzyme

Jason J. Churchill, Stephen C. Kowalczykowski

Research output: Contribution to journalArticle

30 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)537-542
Number of pages6
JournalJournal of Molecular Biology
Volume297
Issue number3
DOIs
StatePublished - Mar 31 2000

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Exodeoxyribonuclease V
Rec A Recombinases
Genetic Recombination
Enzymes
Single-Stranded DNA
DNA
Protein Domains
Escherichia coli

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 journalArticle

Churchill, Jason J. ; Kowalczykowski, Stephen C. / Identification of the RecA protein-loading domain of RecBCD enzyme. In: Journal of Molecular Biology. 2000 ; Vol. 297, No. 3. pp. 537-542.
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