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RecA Dimers Serve as a Functional Unit for Assembly of Active Nucleoprotein Filaments
- Source :
- Biochemistry. 45:13537-13542
- Publication Year :
- 2006
- Publisher :
- American Chemical Society (ACS), 2006.
-
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 as well as their coordinated activity during the catalysis of homologous recombination.
- Subjects :
- Adenosine Triphosphatases
DNA repair
Recombinant Fusion Proteins
RAD51
macromolecular substances
biochemical phenomena, metabolism, and nutrition
Biology
Biochemistry
Molecular biology
Article
Nucleoprotein
Protein filament
Rec A Recombinases
chemistry.chemical_compound
Nucleoproteins
chemistry
Recombinase
Biophysics
bacteria
Repressor lexA
Homologous recombination
Dimerization
DNA
Subjects
Details
- ISSN :
- 15204995 and 00062960
- Volume :
- 45
- Database :
- OpenAIRE
- Journal :
- Biochemistry
- Accession number :
- edsair.doi.dedup.....a7838c72d3a61bf277d0a3f27908dac7