Role of tryptophan 54 in the binding of E. coli single-stranded DNA-binding protein to single-stranded polynucleotides |
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Authors: | M I Khamis J R Casas-Finet A H Maki J B Murphy J W Chase |
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Institution: | 1. Department of Chemistry, University of California, Davis CA 95616 USA;2. Department of Molecular Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA |
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Abstract: | 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. |
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