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Biochemical characterization and cooperation with co-chaperones of heat shock protein 90 from Schizosaccharomyces pombe

Paper ID Volume ID Publish Year Pages File Format Full-Text
20658 43185 2013 5 PDF Available
Title
Biochemical characterization and cooperation with co-chaperones of heat shock protein 90 from Schizosaccharomyces pombe
Abstract

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.

Keywords
Chaperone; Hsp90; Co-chaperone; Conformational change; Schizosaccharomyces pombe
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Biochemical characterization and cooperation with co-chaperones of heat shock protein 90 from Schizosaccharomyces pombe
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 116, Issue 4, October 2013, Pages 444–448
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us