Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity

Hsp90 is an essential and highly conserved modular molecular chaperone whose N and middle domains are separated by a disordered region termed the charged linker. Although its importance has been previously disregarded, because a minimal linker length is sufficient for Hsp90 activity, the evolutionar...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2012-02, Vol.109 (8), p.2937-2942
Hauptverfasser:	Tsutsumi, Shinji, Mollapour, Mehdi, Prodromou, Chrisostomos, Lee, Chung-Tien, Panaretou, Barry, Yoshida, Soichiro, Mayer, Matthias P, Neckers, Leonard M
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine triphosphatase Adenosine triphosphatases adenosinetriphosphatase Amides Amino Acid Sequence Amino acids Biological Sciences Deuterium - metabolism Eukaryotes eukaryotic cells Eukaryotic Cells - metabolism Evolutionary biology Heat shock proteins HSP90 Heat-Shock Proteins - chemistry HSP90 Heat-Shock Proteins - metabolism Humans Hydrogen Molecular Sequence Data Molecular structure Peptide Hydrolases - metabolism Plasmids Plasmodium Protein Binding Proteins Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Solvents Structure-Activity Relationship Viability Yeasts
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