[NMR paper] Monitoring the interaction between ?2-microglobulin and the molecular chaperone ?B-crystallin by NMR and mass spectrometry. ?B-Crystallin dissociates ?2-microglobulin oligomers.
Monitoring the interaction between ?2-microglobulin and the molecular chaperone ?B-crystallin by NMR and mass spectrometry. ?B-Crystallin dissociates ?2-microglobulin oligomers.
Related ArticlesMonitoring the interaction between ?2-microglobulin and the molecular chaperone ?B-crystallin by NMR and mass spectrometry. ?B-Crystallin dissociates ?2-microglobulin oligomers.
J Biol Chem. 2013 May 3;
Authors: Esposito G, Garvey M, Alverdi V, Pettirossi F, Corazza A, Fogolari F, Polano M, Mangione PP, Giorgetti S, Stoppini M, Rekas A, Bellotti V, Heck AJ, Carver JA
Abstract
The interaction at neutral pH between wild-type and a variant form (R3A) of the amyloid fibril-forming protein ?2-microglobulin (?2m) and the molecular chaperone ?B-crystallin was investigated by Thioflavin T fluorescence, NMR spectroscopy and mass spectrometry. Fibril formation of R3A?2m was potently prevented by ?B-crystallin. ?B-crystallin also prevented the unfolding and non-fibrillar aggregation of R3A?2m. From analysis of NMR spectra collected at various R3A?2m to ?B-crystallin molar subunit ratios, it is concluded that the structured ?-sheet core and the apical loops of R3A?2m interact in a non-specific manner with ?B-crystallin. Complementary information was derived from NMR diffusion coefficient measurements of wild-type ?2m at a 100-fold concentration excess with respect to ?B-crystallin. Mass spectrometry acquired in the native state showed that the onset of wild-type ?2m oligomerization was effectively reduced by ?B-crystallin. Furthermore, and most importantly, ?B-crystallin reversibly dissociated ?2m oligomers formed spontaneously in aged samples. These results, coupled with our previous studies, highlight the potent effectiveness of ?B-crystallin in preventing ?2m 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.
PMID: 23645685 [PubMed - as supplied by publisher]
Probing Dynamic Conformationsof the High-Molecular-Weight?B-Crystallin Heat Shock Protein Ensemble by NMR Spectroscopy
Probing Dynamic Conformationsof the High-Molecular-Weight?B-Crystallin Heat Shock Protein Ensemble by NMR Spectroscopy
Andrew J. Baldwin, Patrick Walsh, D. Flemming Hansen, Gillian R. Hilton, Justin L. P. Benesch, Simon Sharpe and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja307874r/aop/images/medium/ja-2012-07874r_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja307874r
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/qcs9RnHBiBY
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Kinetic Intermediates of ?(2)-Microglobulin Fibril Elongation Probed by Pulse-Labelin
Kinetic Intermediates of ?(2)-Microglobulin Fibril Elongation Probed by Pulse-Labeling H/D Exchange Combined with NMR Analysis.
Related Articles Kinetic Intermediates of ?(2)-Microglobulin Fibril Elongation Probed by Pulse-Labeling H/D Exchange Combined with NMR Analysis.
J Mol Biol. 2010 Nov 22;
Authors: Konuma T, Chatani E, Yagi M, Sakurai K, Ikegami T, Naiki H, Goto Y
Amyloid fibril elongation of denatured proteins is considered to involve cycles of coupled binding and misfolding. To gain insights into the possible kinetic intermediate(s), we...
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[NMR paper] Dynamics in the unfolded state of beta2-microglobulin studied by NMR.
Dynamics in the unfolded state of beta2-microglobulin studied by NMR.
Related Articles Dynamics in the unfolded state of beta2-microglobulin studied by NMR.
J Mol Biol. 2005 Feb 11;346(1):279-94
Authors: Platt GW, McParland VJ, Kalverda AP, Homans SW, Radford SE
Many proteins form amyloid-like fibrils in vitro under conditions that favour the population of partially folded conformations or denatured state ensembles. Characterising the structural and dynamic properties of these states is crucial towards understanding the mechanisms of...
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[NMR paper] The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studie
The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR.
Related Articles The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR.
Protein Sci. 2002 Sep;11(9):2218-29
Authors: Katou H, Kanno T, Hoshino M, Hagihara Y, Tanaka H, Kawai T, Hasegawa K, Naiki H, Goto Y
beta(2)-Microglobulin (beta2-m) is a major component of dialysis-related amyloid fibrils. Although recombinant beta2-m forms needle-like fibrils by in vitro extension reaction at pH...
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[NMR paper] NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and c
NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins.
Related Articles NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins.
Int J Biol Macromol. 1998 May-Jun;22(3-4):197-209
Authors: Carver JA, Lindner RA
The subunit molecular mass of alpha-crystallin, like many small heat-shock proteins (sHsps), is around 20 kDa although the protein exists as a large aggregate of average mass around 800...
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[NMR paper] 1H-NMR spectroscopy of beta B2-crystallin from bovine eye lens. Conformation of the N
1H-NMR spectroscopy of beta B2-crystallin from bovine eye lens. Conformation of the N- and C-terminal extensions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H-NMR spectroscopy of beta B2-crystallin from bovine eye lens. Conformation of the N- and C-terminal extensions.
Eur J Biochem. 1993 Apr 1;213(1):313-20
Authors: Carver JA, Cooper PG, Truscott RJ
1H-NMR spectroscopic studies of a 46-kDa homodimer, beta B2-crystallin,...
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[NMR paper] 1H NMR assignments and secondary structure of human beta 2-microglobulin in solution.
1H NMR assignments and secondary structure of human beta 2-microglobulin in solution.
Related Articles 1H NMR assignments and secondary structure of human beta 2-microglobulin in solution.
Biochemistry. 1992 Sep 22;31(37):8906-15
Authors: Okon M, Bray P, VuceliÄ? D
Sequence-specific resonance assignments of human beta 2-microglobulin (M(r) 12,000) and its secondary structure are determined by 2D NMR techniques. The protein is found to contain two antiparallel beta-sheets each of four beta-strands with the beta-sheets being connected by a...
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[NMR paper] Probing the structure and interactions of crystallin proteins by NMR spectroscopy.
Probing the structure and interactions of crystallin proteins by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Probing the structure and interactions of crystallin proteins by NMR spectroscopy.
Prog Retin Eye Res. 1999 Jul;18(4):431-62
Authors: Carver JA
The lens is composed primarily of proteins, the crystallins, at high concentration whose structure and interactions are responsible for lens transparency. As there is no protein turnover in the...
Monitoring the interaction between ?2-microglobulin and the molecular chaperone ?B-crystallin by NMR and mass spectrometry. ?B-Crystallin dissociates ?2-microglobulin oligomers.
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