Small heat shock protein Hsp27 protects myosin S1 from heat-induced aggregation, but not from thermal denaturation and ATPase inactivation
Abstract
We applied different methods, such as turbidity measurements, dynamic light scattering, differential scanning calorimetry and co-sedimentation assay, to analyze the interaction of small heat shock protein Hsp27 with isolated myosin head (myosin subfragment 1, S1) under heat-stress conditions. Upon heating at 43
°C, Hsp27 effectively suppresses S1 aggregation, and this effect is enhanced by mutations mimicking Hsp27 phosphorylation. However, Hsp27 was unable to prevent thermal unfolding of myosin heads and to maintain their ATPase activity under heat-shock conditions.
Structured summary
Keywords: Myosin subfragment 1, Small heat shock proteins, Thermal denaturation, Protein aggregation, Differential scanning calorimetry, Dynamic light scattering
Abbreviations: DLS, dynamic light scattering, DSC, differential scanning calorimetry, Hsp27, recombinant human heat shock protein with apparent molecular mass 27kDa, Hsp27 wt, wild type Hsp27, Hsp27-3D, pseudophosphorylated Hsp27 with mutations S15D, S78D and S82D, sHSP, small heat shock proteins, S1, myosin subfragment 1
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PII: S0014-5793(08)00271-8
doi:10.1016/j.febslet.2008.03.035
© 2008 Federation of European Biochemical Societies
Refers to corrigendum:
- Corrigendum to “Small heat shock protein Hsp27 protects myosin S1 from heat-induced aggregation, but not from thermal denaturation and ATPase inactivation” [FEBS Lett. 582 (2008) 1407–1412] , 06 February 2009
