Role of tryptophan 54 in the binding of E. coli single‐stranded DNA‐binding protein to single‐stranded polynucleotides
[摘要] Fluorescence and optical detection of triplet state magnetic resonance spectroscopy have been employed to study the complexes formed by single-stranded polynucleotides with both E. coli single-stranded DNA-binding protein and an E. coli ssb gene product in which Trp-54 is replaced by phenylalanine using site specific oligonucleotide mutagenesis. Our results strongly suggest the involvement of Trp-54 in stabilizing the protein-nucleic acid complexes via stacking interactions of the aromatic residue with the nucleotide bases.
[发布日期] [发布机构]
[效力级别] [学科分类] 生物化学/生物物理
[关键词] ODMR spectroscopy;Single-stranded DNA binding protein;Stacking interaction;Zero field splitting;Heavy atom effect;Eco SSB;single-stranded DNA-binding protein encoded by E. coli;Eco SSB-Phe 54;single-stranded DNA-binding protein with Trp-54 replaced by Phe;encoded by a cloned ssb gene modified by site specific oligonucleotide mutagenesis;ODMR;optically detected triplet state magnetic resonance;poly(dT);polydeoxythymidylic acid;poly(5-BrU);brominated polyuridylic acid;poly(5-HgU);mercurated polyuridylic acid [时效性]
