Osmolyte-induced conformational changes in the Hsp90 molecular chaperone
نویسندگان
چکیده
منابع مشابه
Osmolyte-induced conformational changes in the Hsp90 molecular chaperone.
Osmolytes are small molecules that play a central role in cellular homeostasis and the stress response by maintaining protein thermodynamic stability at controlled levels. The underlying physical chemistry that describes how different osmolytes impact folding free energy is well understood, however little is known about their influence on other crucial aspects of protein behavior, such as nativ...
متن کاملConformational dynamics of the molecular chaperone Hsp90.
The ubiquitous molecular chaperone Hsp90 makes up 1-2% of cytosolic proteins and is required for viability in eukaryotes. Hsp90 affects the folding and activation of a wide variety of substrate proteins including many involved in signaling and regulatory processes. Some of these substrates are implicated in cancer and other diseases, making Hsp90 an attractive drug target. Structural analyses h...
متن کاملOsmolyte-induced changes in protein conformational equilibria.
Examining solute-induced changes in protein conformational equilibria is a long-standing method for probing the role of water in maintaining protein stability. Interpreting the molecular details governing the solute-induced effects, however, remains controversial. We present experimental and theoretical data for osmolyte-induced changes in the stabilities of the A and N states of yeast iso-1-fe...
متن کاملConformational switching of the molecular chaperone Hsp90 via regulated phosphorylation.
Hsp90 is an essential molecular chaperone in the eukaryotic cytosol. Its function is modulated by cochaperones and posttranslational modifications. Importantly, the phosphatase Ppt1 is a dedicated regulator of the Hsp90 chaperone system. Little is known about Ppt1-dependent phosphorylation sites and how these affect Hsp90 activity. Here, we identified the major phosphorylation sites of yeast Hs...
متن کاملSubstrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone.
Hsp90 is a ubiquitous molecular chaperone. Previous structural analysis demonstrated that Hsp90 can adopt a large number of structurally distinct conformations; however, the functional role of this flexibility is not understood. Here we investigate the structural consequences of substrate binding with a model system in which Hsp90 interacts with a partially folded protein (Δ131Δ), a well-studie...
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ژورنال
عنوان ژورنال: Protein Science
سال: 2009
ISSN: 0961-8368,1469-896X
DOI: 10.1002/pro.282