Journal
PROTEIN SCIENCE
Volume 13, Issue 1, Pages 134-144Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1110/ps.03264204
Keywords
small heat shock protein; archaea; thermoacidophile; chaperone activity; oligomerization
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We expressed and characterized two sHsps, StHsp19.7 and StHsp14.0, from a thermoacidophilic crenarchaeon, Sulfolobus tokodaii strain 7. StHsp19.7 forms a filamentous structure consisting of spherical particles and lacks molecular chaperone activity. Fractionation of Sulfolobus extracts by size exclusion chromatography with immunoblotting indicates that StHsp19.7 exists as a filamentous structure in vivo. On the other hand, StHsp14.0 exists as a spherical oligomer like other sHsps. It showed molecular chaperone activity to protect thermophilic 3-isopropylmalate dehydrogenase (IPMDH) from thermal aggregation at 87degreesC. StHsp14.0 formed variable-sized complexes with denatured IPMDH at 90degreesC. Using StHsp14.0 labeled with fluorescence or biotin probe and magnetic separation, subunit exchanges between complexes were demonstrated. This is the first report on the filament formation of sHsp and also the high molecular chaperone activity of thermophilic archaeal sHsps.
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