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  Deamidation of the human eye lens protein γS-crystallin accelerates oxidative aging

Norton-Baker, B., Mehrabi, P., Kwok, A. O., Roskamp, K. W., Rocha, M. A., Sprague-Piercy, M. A., et al. (2022). Deamidation of the human eye lens protein γS-crystallin accelerates oxidative aging. Structure, 30(5), 763-776. doi:10.1101/2021.06.21.449298.

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https://doi.org/10.1016/j.str.2022.03.002 (Publisher version)
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 Creators:
Norton-Baker, B.1, 2, Author              
Mehrabi, P.2, 3, Author              
Kwok, A. O.1, Author
Roskamp, K. W.1, Author
Rocha, M. A.1, Author
Sprague-Piercy, M. A.4, Author
von Stetten, D.5, Author
Miller, R. J. D.6, Author
Martin, R. W.1, 4, Author
Affiliations:
1Department of Chemistry, University of California, ou_persistent22              
2Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_1938288              
3Institute for Nanostructure and Solid-State Physics, Universität Hamburg, ou_persistent22              
4Department of Molecular Biology and Biochemistry, University of California, ou_persistent22              
5European Molecular Biology Laboratory, Hamburg Unit c/o Deutsches Elektronen-Synchrotron, ou_persistent22              
6Departments of Chemistry and Physics, University of Toronto, ou_persistent22              

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 Abstract: Cataract, a clouding of the eye lens from protein precipitation, affects millions of people every year. The lens proteins, the crystallins, show extensive post-translational modifications (PTMs) in cataractous lenses. The most common PTMs, deamidation and oxidation, promote crystallin aggregation; however, it is not clear precisely how these PTMs contribute to crystallin insolubilization. Here, we report six crystal structures of the lens protein γS-crystallin (γS): one of the wild-type and five of deamidated γS variants, from three to nine deamidation sites, after sample aging. The deamidation mutations do not change the overall fold of γS; however, increasing deamidation leads to accelerated disulfide-bond formation. Addition of deamidated sites progressively destabilized protein structure, and the deamidated variants display an increased propensity for aggregation. These results suggest that the deamidated variants are useful as models for accelerated aging; the structural changes observed provide support for redox activity of γS-crystallin in the lens.

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Language(s): eng - English
 Dates: 2021-12-142021-06-192022-03-012022-03-252022-05-05
 Publication Status: Published in print
 Pages: 14
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 Table of Contents: -
 Rev. Type: Peer
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Title: Structure
  Other : Structure
Source Genre: Journal
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Publ. Info: London : Cell Press
Pages: - Volume / Issue: 30 (5) Sequence Number: - Start / End Page: 763 - 776 Identifier: ISSN: 0969-2126
CoNE: https://pure.mpg.de/cone/journals/resource/954927002244_1