title: Modulation of the chaperone activities of Hsc70/Hsp40 by Hsp105alpha and Hsp105beta.
abstract: Hsp105alpha and Hsp105beta are stress proteins found in various mammals including human, mouse, and rat, which belong to the Hsp105/Hsp110 protein family. To elucidate their physiological functions, we examined here the chaperone activity of these stress proteins. Hsp105alpha and Hsp105beta prevented the aggregation of firefly luciferase during thermal denaturation, whereas the thermally denatured luciferase was not reactivated by itself or by rabbit reticulocyte lysate (RRL). On the other hand, Hsp105alpha and Hsp105beta suppressed the reactivation of thermally denatured luciferase by RRL and of chemically denatured luciferase by Hsc70/Hsp40 or RRL. Furthermore, although Hsp105alpha and Hsp105beta did not show ATPase activity, the addition of Hsp105alpha or Hsp105beta to Hsc70/Hsp40 enhanced the amount of hydrolysis of ATP greater than that of the Hsp40-stimulated Hsc70 ATPase activity. These findings suggest that Hsp105alpha and Hsp105beta are not only chaperones that prevent thermal aggregation of proteins, but also regulators of the Hsc70 chaperone system in mammalian cells.
authors.affiliation: Department of Biochemistry, Kyoto Pharmaceutical University, 5 Nakauchi-cho, Misasagi, Yamashina-ku, Kyoto, Japan.
authors.forename: N
authors.initials: N
authors.lastname: Yamagishi
authors.forename: H
authors.initials: H
authors.lastname: Nishihori
authors.forename: K
authors.initials: K
authors.lastname: Ishihara
authors.forename: K
authors.initials: K
authors.lastname: Ohtsuka
authors.forename: T
authors.initials: T
authors.lastname: Hatayama
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism / Q000494:pharmacology; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D002457:Cell Extracts / Q000494:pharmacology; D004305:Dose-Response Relationship, Drug; D004789:Enzyme Activation / Q000187:drug effects; D050883:HSC70 Heat-Shock Proteins; D050957:HSP110 Heat-Shock Proteins; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism* / Q000494:pharmacology; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006358:Hot Temperature; D006801:Humans; D006868:Hydrolysis / Q000187:drug effects; D008156:Luciferases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding / Q000187:drug effects; D011489:Protein Denaturation / Q000187:drug effects; D017510:Protein Folding; D020673:Protein Renaturation / Q000187:drug effects; D011993:Recombinant Fusion Proteins / Q000378:metabolism / Q000494:pharmacology; D012156:Reticulocytes / Q000166:cytology
chemical_list: D002352:Carrier Proteins; D002457:Cell Extracts; C494647:DNAJB1 protein, human; D050883:HSC70 Heat-Shock Proteins; D050957:HSP110 Heat-Shock Proteins; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; C494371:HSPA8 protein, human; C097205:HSPH1 protein, human; D006360:Heat-Shock Proteins; C490783:Hsp105 protein, mouse; C494373:Hspa8 protein, rat; D011993:Recombinant Fusion Proteins; D000255:Adenosine Triphosphate; D008156:Luciferases; D000251:Adenosine Triphosphatases