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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
Published on: June 7, 2018
pH-induced changes of the structure of small heat shock proteins with molecular mass 24/27kDa (HspB1)
Ivan S Chernik1, Olesya O Panasenko, Yi Li
1Department of Biochemistry, School of Biology, Moscow State University, Moscow 119992, Russia.
Abstract:
The effect of pH on the structure of recombinant chicken Hsp24, human Hsp27 and their 3D mutants mimicking phosphorylation at Ser15, Ser77/78, and Ser81/82 was analyzed. Circular dichroism and fluorescent spectroscopy indicate that changes of pH in the range 6.0-7.5 weakly affected the secondary and tertiary structure of the wild type proteins, but induced noticeable changes in the structure of their 3D mutants. According to size-exclusion chromatography and analytical ultracentrifugation variation of pH-induced pronounced changes in the quaternary structure of small heat shock proteins and acidification resulted in accumulation of large oligomers of Hsp24/27. It is concluded that small changes of pH strongly affect the quaternary structure of small heat shock proteins and by this means can influence their functioning in the cell.
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