RecA dimers serve as a functional unit for assembly of active nucleoprotein filaments
Authors
Forget, Anthony L.Kudron, Michelle M.
McGrew, Dharia A.
Calmann, Melissa A.
Schiffer, Celia A.
Knight, Kendall L.
UMass Chan Affiliations
Department of Biochemistry and Molecular PharmacologyDocument Type
Journal ArticlePublication Date
2006-11-08Keywords
Adenosine TriphosphatasesDimerization
Nucleoproteins
Rec A Recombinases
Recombinant Fusion Proteins
Biochemistry, Biophysics, and Structural Biology
Pharmacology, Toxicology and Environmental Health
Metadata
Show full item recordAbstract
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.Source
Biochemistry. 2006 Nov 14;45(45):13537-42. Link to article on publisher's siteDOI
10.1021/bi060938qPermanent Link to this Item
http://hdl.handle.net/20.500.14038/26138PubMed ID
17087507Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1021/bi060938q