N- and C-terminal regions of ?B-crystallin and Hsp27 mediate inhibition of amyloid nucleation, fibril binding, and fibril disaggregation
Emily E Selig, Courtney O Zlatic, Dezerae Cox, Yee-Foong Mok, Paul R Gooley, Heath Ecroyd, Michael DW Griffin
JOURNAL OF BIOLOGICAL CHEMISTRY | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2020
Small heat-shock proteins (sHSPs) are ubiquitously expressed molecular chaperones that inhibit amyloid fibril formation; however, their mechanisms of action remain poorly understood. sHSPs comprise a conserved α-crystallin domain flanked by variable N- and C-terminal regions. To investigate the functional contributions of these three regions, we compared the chaperone activities of various constructs of human αB-crystallin (HSPB5) and heat-shock 27-kDa protein (Hsp27, HSPB1) during amyloid formation by α-synuclein and apolipoprotein C-II. Using an array of approaches, including thioflavin T fluorescence assays and sedimentation analysis, we found that the N-terminal region of Hsp27 and the t..View full abstract
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Awarded by Australian Research Council
E. E. S. is the recipient of an Australian Government Research Training Program Scholarship. M. D. W. G. is the recipient of Australian Research Council Future Fellowship FT140100544.