The RecA binding locus of RecBCD is a general domain for recruitment of DNA strand exchange proteins

Maria Spies, Stephen C. Kowalczykowski

Research output: Contribution to journalArticle

71 Citations (Scopus)

Abstract

RecBCD enzyme facilitates loading of RecA protein onto ssDNA produced by its helicase/nuclease activity. This process is essential for RecBCD-mediated homologous recombination. Here, we establish that the C-terminal nuclease domain of the RecB subunit (RecBnuc) forms stable complexes with RecA. Interestingly, RecBnuc also interacts with and loads noncognate DNA strand exchange proteins. Interaction is with a conserved element of the RecA-fold, but because the binding to noncognate proteins decreases in a phylogenetically consistent way, species-specific interactions are also present. RecBnuc does not impede activities of RecA that are important to DNA strand exchange, consistent with its role in targeting of RecA. Modeling predicts the interaction interface for the RecA-RecBCD complex. Because a similar interface is involved in the binding of human Rad51 to the conserved BRC repeat of BRCA2 protein, the RecB-domain may be one of several structural domains that interact with and recruit DNA strand exchange proteins to DNA.

Original languageEnglish (US)
Pages (from-to)573-580
Number of pages8
JournalMolecular Cell
Volume21
Issue number4
DOIs
StatePublished - Feb 17 2006

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DNA
Exodeoxyribonuclease V
BRCA2 Protein
Proteins
Rec A Recombinases
Homologous Recombination
deoxyribonuclease C
Protein Domains

ASJC Scopus subject areas

  • Molecular Biology

Cite this

The RecA binding locus of RecBCD is a general domain for recruitment of DNA strand exchange proteins. / Spies, Maria; Kowalczykowski, Stephen C.

In: Molecular Cell, Vol. 21, No. 4, 17.02.2006, p. 573-580.

Research output: Contribution to journalArticle

Spies, Maria ; Kowalczykowski, Stephen C. / The RecA binding locus of RecBCD is a general domain for recruitment of DNA strand exchange proteins. In: Molecular Cell. 2006 ; Vol. 21, No. 4. pp. 573-580.
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