Self-association of phosphorylase kinase from rabbit skeletal muscles under conditions close to those of an intracellular environment

Merem’yanin, A. V.; Chebotareva, Natalia A.; Makeeva, Valentina F.; Bi, Kurganov

doi:10.1134/s1607672907040059

Cited by 3 publications

(1 citation statement)

References 11 publications

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“…The PhK with molecular mass of 1 320 kDa4 has a complex molecular organization and consists of four subunits that form a hexadecamer (αβγδ) 4 , where the γ‐subunit possesses the catalytic activity and α‐, β‐, and δ‐subunits regulate its activity 4–7. Ca 2+ and Mg 2+ stimulate the PhK activity by inducing changes in the tertiary and quaternary structure of the molecule5–9 and also stimulate hexadecamer association 10–13…”

Section: Introductionmentioning

confidence: 99%

Interaction of Hsp27 with Native Phosphorylase Kinase under Crowding Conditions

Chebotareva

Makeeva

Bazhina

et al. 2010

Macromolecular Bioscience

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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.

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