tailieunhanh - Báo cáo khoa học: Interaction of the small heat shock protein with molecular mass 25 kDa (hsp25) with actin

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 actinwas analyzedbymeans of fluorescence spectroscopy and ultracentrifugation. Wild typeHSP25 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 C was partially denatured, but retained its ability to polymerize | Eur. J. Biochem. 270 892-901 2003 FEBS 2003 doi Interaction of the small heat shock protein with molecular mass 25 kDa hsp25 with actin Olesya O. Panasenko1 Maria V. Kim1 Steven B. Marston2 and Nikolai B. Gusev1 1 Department of Biochemistry School of Biology Moscow State University Moscow Russia imperial College School of Medicine at National Heart and Lung Institute Dovehose Street London UK 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 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 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. Keywords small heat shock protein actin thermal denaturation. Actin is the major component of the thin filaments of muscle cells and of the cytoskeleton system of nonmuscle cells. It is therefore a very abundant protein and its concentration in smooth muscle is close to 800-900 M 1 . Actin has a rather complex and .

TỪ KHÓA LIÊN QUAN
crossorigin="anonymous">
Đã phát hiện trình chặn quảng cáo AdBlock
Trang web này phụ thuộc vào doanh thu từ số lần hiển thị quảng cáo để tồn tại. Vui lòng tắt trình chặn quảng cáo của bạn hoặc tạm dừng tính năng chặn quảng cáo cho trang web này.