NDLI: Monitoring the Interaction between β2-Microglobulin and the Molecular Chaperone αB-crystallin by NMR and Mass Spectrometry αB-CRYSTALLIN DISSOCIATES β2-MICROGLOBULIN OLIGOMERS

Content Provider	Journal of Biological Chemistry (JBC)
Author	Esposito, Gennaro Garvey, Megan Alverdi, Vera Pettirossi, Fabio Corazza, Alessandra Fogolari, Federico Polano, Maurizio Mangione, P. Patrizia Giorgetti, Sofia Stoppini, Monica Rekas, Agata Bellotti, Vittorio Heck, Albert J. R. Carver, John A.
Abstract	The interaction at neutral pH between wild-type and a variant form (R3A) of the amyloid fibril-forming protein β2-microglobulin (β2m) and the molecular chaperone αB-crystallin was investigated by thioflavin T fluorescence, NMR spectroscopy, and mass spectrometry. Fibril formation of R3Aβ2m was potently prevented by αB-crystallin. αB-crystallin also prevented the unfolding and nonfibrillar aggregation of R3Aβ2m. From analysis of the NMR spectra collected at various R3Aβ2m to αB-crystallin molar subunit ratios, it is concluded that the structured β-sheet core and the apical loops of R3Aβ2m interact in a nonspecific manner with the αB-crystallin. Complementary information was derived from NMR diffusion coefficient measurements of wild-type β2m at a 100-fold concentration excess with respect to αB-crystallin. Mass spectrometry acquired in the native state showed that the onset of wild-type β2m oligomerization was effectively reduced by αB-crystallin. Furthermore, and most importantly, αB-crystallin reversibly dissociated β2m oligomers formed spontaneously in aged samples. These results, coupled with our previous studies, highlight the potent effectiveness of αB-crystallin in preventing β2m aggregation at the various stages of its aggregation pathway. Our findings are highly relevant to the emerging view that molecular chaperone action is intimately involved in the prevention of in vivo amyloid fibril formation.
Related Links	http://www.jbc.org/content/288/24/17844.abstract
Ending Page	17858
Starting Page	17844
Page Count	15
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	24
Volume Number	288
DOI	10.1074/jbc.M112.448639
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2013-06-14
Access Restriction	Open
Subject Keyword	Amyloid Mass Spectrometry (MS) Nuclear Magnetic Resonance Protein Aggregation Small Heat Shock Proteins Amyloid Fibrils NMR Spectroscopy ΑB-crystallin Β2-Microglobulin Native Mass Spectrometry Protein Structure and Folding
Alternative Title	Monitoring the Interaction between β2-Microglobulin and the Molecular Chaperone αB-crystallin by NMR and Mass Spectrometry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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