Biochemical characterization and cooperation with co-chaperones of heat shock protein 90 from Schizosaccharomyces pombe(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

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概要

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• The characterization of Hsp90 from the fission yeast Schizosaccharomyces pombe was performed. Hsp90 of S. pombe existed as a dimer and exhibited ATP-dependent conformational changes. It captured unfolded proteins in the ATP-free open conformation and protected them from thermal aggregation. Hsp90 of S. pombe was also able to refold thermally denatured firefly luciferase. The co-chaperones Sti1 and Aha1 bound Hsp90 and modulated its activity. Because the affinity of Sti1 was higher than that of Aha1, the effect of Sti1 appeared to dominate when both co-chaperones existed simultaneously.

著者

• Yohda Masafumi

  Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology

• Yohda Masafumi

  Department Of Biotechnology And Life Science Graduate School Of Engineering Tokyo University Of Agri

• Ishida Mari

  Department Of Cardiovascular Physiology And Medicine Graduate School Of Biomedical Sciences Hiroshim

• Kanzaki Taro

  Department Of Biotechnology And Life Science Tokyo University Of Agriculture And Technology

• Oka Toshihiko

  Departemnt Of Organic Chemistry And Biochemistry Institute Of Scientific And Iindustrial Research Os

• Abe Tetsuya

  Department Of Biochemistry School Of Medicine University Of Occupational And Environmental Health

• Abe Tetsuya

  Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology

• Tomomari Taichi

  Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology

• Ishida Mari

  Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology

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