Interaction of Hsp27 with Native Phosphorylase Kinase under Crowding Conditions
Interaction of Hsp27 with Native Phosphorylase Kinase under Crowding Conditions
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DOI：
10.1002/mabi.200900397
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发表时间：
2010-07-07
影响因子：
4.6
通讯作者：
Kurganov, Boris I.
中科院分区：
文献类型：
--
作者：
Chebotareva, Natalia A.;Makeeva, Valentina F.;Kurganov, Boris I.
在模拟拥挤条件下，研究了野生型(Wt)热休克蛋白Hsp27及其三维突变体(模仿Ser15、78和82位的磷酸化)与兔骨骼肌磷酸酶激酶(PhK)的相互作用。根据沉积速度和动态光散射数据，拥挤引发了PHK和HSP27的大尺寸缔合的形成。在拥挤的条件下，PhK和Hsp27的小分子相互作用，从而导致每个蛋白质的大的同源低聚物解离。考虑到细胞内高浓度的PhK，我们推测天然PhK可能调节了Hsp27的低聚状态和伴侣样活性。
Interaction of the wild type (wt) heat shock protein Hsp27 and its three-dimensional (3D) mutant (mimicking phosphorylation at Ser15, 78, and 82) with rabbit skeletal muscle phosphorylase kinase (PhK) has been studied under crowding conditions modeled by addition of 1 M trimethylamine N-oxide (TMAO). According to the data of sedimentation velocity and dynamic light scattering, crowding provokes the formation of large-sized associates of both PhK and Hsp27. Under crowding conditions, small associates of PhK and Hsp27 interact with each other thus leading to dissociation of large homooligomers of each protein. Taking into account high concentrations of PhK in the cell, we speculate that native PhK might modulate the oligomeric state and chaperone-like activity of Hsp27.