Small heat shock protein Hsp27 protects myosin S1 from heat-induced aggregation, but not from thermal denaturation and ATPase inactivation

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 degrees 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: MINT-6490863, MINT-6490872: LC1 (S1) (uniprotkb: P02602), Myosin subfragment 1 ( S1) ( uniprotkb: P02562) and Hsp27 ( uniprotkb: P04792) physically interact (MI: 0218) by dynamic light scattering ( MI: 0038) MINT-6490833: LC1 ( S1) ( uniprotkb: P02602), Myosin subfragment 1 ( S1) ( uniprotkb: P02562) and Hsp27 ( uniprotkb: P04792) physically interact ( MI: 0218) by cosedimentation ( MI: 0027) MINT-6490770, MINT-6490782: LC1 ( S1) ( uniprotkb: P02602), Myosin subfragment 1 ( S1) ( uniprotkb: P02562) and Hsp27 ( uniprotkb: P04792) physically interact ( MI: 0218) by light scattering ( MI: 0067) (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.