Interaction of Hsp27 with Native Phosphorylase Kinase under Crowding Conditions

• Published in: Macromolecular bioscience Vol. 10; no. 7; pp. 783 - 789
• Main Authors: Chebotareva, Natalia A., Makeeva, Valentina F., Bazhina, Svetlana G., Eronina, Tatyana B., Gusev, Nikolai B., Kurganov, Boris I.
• Format: Journal Article
• Language: English
• Published: Weinheim WILEY-VCH Verlag 07.07.2010; WILEY‐VCH Verlag
• Subjects: analytical ultracentrifugation; Animals; Chemical Fractionation; Crowding; Heat shock proteins; Hsp27; HSP27 Heat-Shock Proteins - metabolism; Humans; Kinases; light scattering; Macromolecular Substances - metabolism; Muscles; Mutant Proteins - metabolism; phosphorylase kinase; Phosphorylase Kinase - metabolism; Phosphorylases; Protein Binding; Rabbits; Sedimentation; self-assembly; Three dimensional; Trimethylamine; Ultracentrifugation
• ISSN: 1616-5187; 1616-5195
• DOI: 10.1002/mabi.200900397

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. Interaction of the wild type Hsp27 and its 3D phosphomimic mutant with rabbit muscle phosphorylase kinase (PhK) has been studied under crowding conditions induced by 1 M trimethylamine N‐oxide. Under crowding conditions PhK interacts with small oligomers of Hsp27 to form stable complexes and by this means induces dissociation of large Hsp27 oligomers. It is speculated that by these means native PhK might regulate the chaperone‐like activity of small heat shock proteins.