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Interaction of the small heat shock protein with molecular mass 25 kDa (hsp25) with actin.
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
2003 (English)In: European Journal of Biochemistry, ISSN 0014-2956, E-ISSN 1432-1033, Vol. 270, no 5Article in journal (Refereed) Published
Abstract [en]

The interaction of heat shock protein with molecular mass 25 kDa (HSP25) and its point mutants S77D + S81D (2D mutant) and S15D + S77D + S81D (3D mutant) with intact and thermally denatured actin was analyzed by means of fluorescence spectroscopy and ultracentrifugation. Wild type HSP25 did not affect the polymerization of intact actin. The HSP25 3D mutant decreased the initial rate without affecting the maximal extent of intact actin polymerization. G-actin heated at 40-45 degrees C was partially denatured, but retained its ability to polymerize. The wild type HSP25 did not affect polymerization of this partially denatured actin. The 3D mutant of HSP25 increased the initial rate of polymerization of partially denatured actin. Heating at more than 55 degrees C induced complete denaturation of G-actin. Completely denatured G-actin cannot polymerize, but it aggregates at increased ionic strength. HSP25 and especially its 2D and 3D mutants effectively prevent salt-induced aggregation of completely denatured actin. It is concluded that the interaction of HSP25 with actin depends on the state of both actin and HSP25. HSP25 predominantly acts as a chaperone and preferentially interacts with thermally unfolded actin, preventing the formation of insoluble aggregates.

Place, publisher, year, edition, pages
2003. Vol. 270, no 5
National Category
Biological Sciences Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-128276PubMedID: 12603322OAI: oai:DiVA.org:umu-128276DiVA, id: diva2:1051097
Available from: 2016-12-01 Created: 2016-12-01 Last updated: 2018-06-09

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Kim, Maria V

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