Role of tryptophan 54 in the binding of E. coli single‐stranded DNA‐binding protein to single‐stranded polynucleotides

FEBS Letters

Khamis, Mustafa I.¹  Casas-Finet, Jose R.¹  Murphy, Janet B.¹  Chase, John W.¹  Maki, August H.¹ 

[1] Department of Chemistry, University of California, Davis CA 95616 USA

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;   

DOI  :  10.1016/0014-5793(87)81427-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown