Article
The carboxyl terminal of the archaeal nuclease NurA is involved in the interaction with single-stranded DNA-binding protein and dimer formation.
Extremophiles : life under extreme conditions - 1 Mar 2011
Wei Tao, Zhang Songtao, Hou Linlin, Ni Jinfeng, Sheng Duohong, Shen Yulong
Abstract excerpt
The nuclease NurA is present in all known thermophilic archaea and has been implicated to facilitate efficient DNA double-strand break end processing in Mre11/Rad50-mediated homologous recombinational repair. To understand the structural and functional relationship of this enzyme, we constructed five site-directed mutants of NurA from Sulfolobus tokodaii (StoNurA), D56A, E114A, D131A, Y291A, and H299A, at the...
Topics
- Amino Acid Motifs
- Amino Acid Sequence
- Archaeal Proteins
- Cross-Linking Reagents
- DNA Repair
- DNA, Single-Stranded
- Dimerization
- Endodeoxyribonucleases
- Exodeoxyribonucleases
- Formaldehyde
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation