[HTML][HTML] Self-association and chaperone activity of Hsp27 are thermally activated
B Lelj-Garolla, AG Mauk - Journal of biological chemistry, 2006 - ASBMB
The small heat shock protein 27 (Hsp27) is an oligomeric, molecular chaperone in vitro. This
chaperone activity and other physiological roles attributed to Hsp27 have been reported to
depend on the state of self-association. In the present work, we have used sedimentation
velocity experiments to demonstrate that the self-association of Hsp27 is independent of pH
and ionic strength but increases significantly as the temperature is increased from 10 to 40°
C. The largest oligomers formed at 10° C are∼ 8-12 mer, whereas at 40° C oligomers as …
chaperone activity and other physiological roles attributed to Hsp27 have been reported to
depend on the state of self-association. In the present work, we have used sedimentation
velocity experiments to demonstrate that the self-association of Hsp27 is independent of pH
and ionic strength but increases significantly as the temperature is increased from 10 to 40°
C. The largest oligomers formed at 10° C are∼ 8-12 mer, whereas at 40° C oligomers as …