Title

RecA dimers serve as a functional unit for assembly of active nucleoprotein filaments

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology

Publication Date

2006-11-08

Document Type

Article

Subjects

Adenosine Triphosphatases; Dimerization; Nucleoproteins; Rec A Recombinases; Recombinant Fusion Proteins

Disciplines

Biochemistry, Biophysics, and Structural Biology | Pharmacology, Toxicology and Environmental Health

Abstract

All RecA-like recombinase enzymes catalyze DNA strand exchange as elongated filaments on DNA. Despite numerous biochemical and structural studies of RecA and the related Rad51 and RadA proteins, the unit oligomer(s) responsible for nucleoprotein filament assembly and coordinated filament activity remains undefined. We have created a RecA fused dimer protein and show that it maintains in vivo DNA repair and LexA co-protease activities, as well as in vitro ATPase and DNA strand exchange activities. Our results support the idea that dimeric RecA is an important functional unit both for assembly of nucleoprotein filaments and for their coordinated activity during the catalysis of homologous recombination.

DOI of Published Version

10.1021/bi060938q

Source

Biochemistry. 2006 Nov 14;45(45):13537-42. Link to article on publisher's site

Journal/Book/Conference Title

Biochemistry

Related Resources

Link to Article in PubMed

PubMed ID

17087507

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