Article
Both OB folds of single-stranded DNA-binding protein are essential for its ssDNA binding activity in Deinococcus radiodurans.
Protein and peptide letters - 1 Oct 2010
Hua Xiaoting, Wang Chao, Zhao Ye, Wang Hu, Huang Lifen, Xu Guangzhi, Li Mingfeng, Wang Yuan, Tian Bing, Hua Yuejin
Abstract excerpt
The single-stranded DNA-binding proteins are crucial in all kinds of DNA metabolic processes. Deinococcus SSB-like proteins are homodimers in nature and contain two OB folds per monomer, in contrast to other bacterial SSB proteins that are functionally active as homotetramers. We generated four truncated variants of DraSSB protein, based on its crystal structure (PDB code: 1SE8). Gel filtration showed that...
Topics
- DNA, Single-Stranded
- DNA-Binding Proteins
- Deinococcus
- Electrophoresis, Polyacrylamide Gel
- Fluorescence Resonance Energy Transfer
- Genetic Variation
- Protein Folding
- Sequence Alignment