Format

Send to

Choose Destination
See comment in PubMed Commons below
Plant Mol Biol. 2008 Nov;68(4-5):479-91. doi: 10.1007/s11103-008-9385-6. Epub 2008 Aug 10.

Homologous recombination properties of OsRad51, a recombinase from rice.

Author information

1
Plant Biochemistry Section, Molecular Biology Division, Bhabha Atomic Research Center, Mumbai 400085, India.

Abstract

cDNA corresponding to OsRad51 protein was isolated from cDNA library of rice flowers (Oryza sativa, Indica cultivar group) and cloned in to pET28a expression vector. The protein was over expressed in E. coli BL21 (DE3) and purified. Purified OsRad51 could bind single and double stranded DNA, however it showed higher affinity for single stranded DNA. Transmission Electron Microscopy (TEM) studies of OsRad51-DNA complexes showed that this protein formed ring like structures and bound DNA forming filaments. OsRad51 protein promoted renaturation of complementary single strands in to duplex DNA molecules and also showed ATPase activity, which was stimulated by single strand DNA. Fluorescence resonance energy transfer (FRET) assays revealed that OsRad51 promoted homology dependent renaturation as well as strand exchange reactions. Renaturation activity was ATP dependent; however strand exchange activity was ATP independent. This is the first report on in vitro characterization of Rad51 protein from crop plants.

PMID:
18695945
DOI:
10.1007/s11103-008-9385-6
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Springer
    Loading ...
    Support Center