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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 h...
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Published in: | FEBS letters 2008-04, Vol.582 (10), p.1407-1412 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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.
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) |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/j.febslet.2008.03.035 |