title: Transient transformation of oligomeric structure of alpha-crystallin during its chaperone action.
abstract: New evidence for dynamic behavior and flexible oligomeric structure of the molecular chaperone α-crystallin is presented. Based on the results of laser dynamic light scattering, centrifugal ultrafiltration, size exclusion chromatography, analytical ultracentrifugation and electrophoresis in polyacrylamide gel, addition of α-crystallin to fully reduced α-lactalbumin, used as a model protein substrate, at the stage of its start aggregate formation results in dissociation of multimeric structure of α-crystallin. In addition to large oligomers, transient low-sized assemblies are formed with the apparent molecular mass of 50-55 kDa that corresponds to the α-crystallin dimeric form associated with destabilized monomeric α-lactalbumin. This phenomenon is suggested to represent an essential component of a transient protective mechanism tuning the stressed protein to binding sites on the exposed surface of the chaperone dimers.
authors.affiliation: Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky Prospect 33, 119071 Moscow, Russia.
authors.forename: Ekaterina
authors.initials: E
authors.lastname: Smirnova
authors.forename: Natalia
authors.initials: N
authors.lastname: Chebotareva
authors.forename: Bella
authors.initials: B
authors.lastname: Gurvits
mesh_terms: D004229:Dithiothreitol / Q000494:pharmacology; D007700:Kinetics; D007768:Lactalbumin / Q000737:chemistry; D018832:Molecular Chaperones / Q000737:chemistry*; D011487:Protein Conformation; D055503:Protein Multimerization / Q000187:drug effects; D038201:alpha-Crystallins / Q000737:chemistry*
chemical_list: D018832:Molecular Chaperones; D038201:alpha-Crystallins; D007768:Lactalbumin; D004229:Dithiothreitol