The thermostability of DNA-binding protein HU from bacilli |
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Authors: | Wilson, Keith S. Vorgias, Constantin E. Tanaka, Isao White, Stephen W. Kimura, Makoto |
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Affiliation: | European Molecular Biology Laboratory (EMBL), c/o DESY Notkestrasse 85, D-2000 Hamburg 52, FRG 1Department of Polymer Science, Hokkaido University Sapporo 006, Japan 2Biology Department, Brookhaven National Laboratory Upton, Long Island, NY 11973, USA 3Max-Planck Institute for Molecular Genetics Ihnestrasse 5253. West Berlin, FRG |
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Abstract: | The primary and tertiary structures of DNA-binding protein HUfrom Bacillus stearothermophilus are already known. The primarystructure has been previously determined for HU from the closelyrelated B.globigü and the determinations of the sequencesfrom B.caldolyticus and B.subtilis are described here. Thesebacteria have optimum growth temperatures of > 70C (B.caldolyticus),65C (B.stearothermophilus), 37C (B.subtilis) and 30C (B.globigü).in vitro measurements from circular dichroic spectra describedhere give Tm values reflecting these growth temperatures, of68, 64, 43 and 41C respectively. We discuss here the relativethermostability of the four proteins in terms of the amino aciddifferences between the sequences and the three-dimensionalmodel of the B.stearothermophilus HU. The current model forthe interaction of the protein with DNA is only discussed interms of its relevance with regard to thermostability. |
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Keywords: | Bacillus/ circular dichroic spectra/ DNA-binding protein HU/ thermostability |
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