Effects of small heat shock proteins on the thermal denaturation and aggregation of F-actin.
Effect of recombinant chicken small heat shock protein with molecular mass 24 kDa (Hsp24) and recombinant human small heat shock protein with molecular mass 27 kDa (Hsp27) on the heat-induced denaturation and aggregation of skeletal F-actin was analyzed by means of differential scanning calorimetry and light scattering. All small heat shock proteins did not affect thermal unfolding of F-actin measured by differential scanning calorimetry, but effectively prevented aggregation of thermally denatured actin. Small heat shock protein formed stable complexes with denatured (but not with intact) F-actin. The size of these highly soluble complexes was smaller than the size of intact F-actin filaments. It is supposed that protective effect of small heat shock proteins on the cytoskeleton is at least partly due to prevention of aggregation of denatured actin.
Pivovarova
Anastasiya V
AV
A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow 119071, Russia.
Mikhailova
Valeria V
VV
Chernik
Ivan S
IS
Chebotareva
Natalia A
NA
Levitsky
Dmitrii I
DI
Gusev
Nikolai B
NB
D000199:Actins / Q000737:chemistry*; D000818:Animals; D002152:Calorimetry, Differential Scanning; D002645:Chickens; D006360:Heat-Shock Proteins / Q000502:physiology*; D006801:Humans; D011489:Protein Denaturation
D000199:Actins; D006360:Heat-Shock Proteins