The interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: A light and X-ray scattering investigation

Justyn W Regini; Heath Ecroyd; Sarah Meehan; Kristen Bremmell; Matthew J Clarke; Donna Lammie; Tim J Wess; John A Carver

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The interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: A light and X-ray scattering investigation

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The interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: A light and X-ray scattering investigation

Justyn W Regini, Heath Ecroyd, Sarah Meehan, Kristen Bremmell, Matthew J Clarke, Donna Lammie, Tim J Wess and John A Carver

Molecular Vision, Vol.16(260-62), pp.2446-2456

2010

PMCID: PMC2998715

PMID: 21152271

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Abstract

Purpose: The molecular chaperone αB-crystallin is found in high concentrations in the lens and is present in all major body tissues. Its structure and the mechanism by which it protects its target protein from aggregating and precipitating are not known. Methods: Dynamic light scattering and X-ray solution scattering techniques were used to investigate structural features of the αB-crystallin oligomer when complexed with target proteins under mild stress conditions, i.e., reduction of α- lactalbumin at 37 °C and malate dehydrogenase when heated at 42 °C. In this investigation, the size, shape and particle distribution of the complexes were determined in real-time following the induction of stress. Results: Overall, it is observed that the mass distribution, hydrodynamic radius, and spherical shape of the αB-crystallin oligomer do not alter significantly when it complexes with its target protein. Conclusions: The data are consistent with the target protein being located in the outer protein shell of the αB-crystallin oligomer where it is readily accessible for possible refolding via the action of other molecular chaperones. © 2010 Molecular Vision.

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Title: The interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: A light and X-ray scattering investigation
Authors: Justyn W Regini (Author) - Cardiff University
Heath Ecroyd (Author) - The University of Adelaide
Sarah Meehan (Author) - University of Cambridge
Kristen Bremmell (Author) - University of South Australia
Matthew J Clarke (Author) - Cardiff University
Donna Lammie (Author) - Cardiff University
Tim J Wess (Author) - Cardiff University
John A Carver (Author) - The University of Adelaide
Publication details: Molecular Vision, Vol.16(260-62), pp.2446-2456
Publisher: Molecular Vision
Date published: 2010
ISSN: 1090-0535
PMID: 21152271; PMC2998715
Copyright note: Copyright © 2010 Molecular Vision. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Grant note: This work was supported by a grant from the Australian Research Council (to J.A.C.). H.E. was a National Health and Medical Research Council Peter Doherty Fellow. S.M. acknowledges the support of a Royal Society Dorothy Hodgkin Fellowship.
Organisation Unit: Office of the Deputy Vice-Chancellor (Academic)
Language: English
Record Identifier: 99451222102621
Output Type: Journal article

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Collaboration types: Domestic collaboration; International collaboration
Web Of Science research areas: Biochemistry & Molecular Biology; Ophthalmology

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