ArticlePloS one2012
Hydroimidazolone modification of the conserved Arg12 in small heat shock proteins: studies on the structure and chaperone function using mutant mimics.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 40 citations in OpenAlex.
- Site-Specific Glycation of Human Heat Shock Protein (Hsp27) Enhances Its Chaperone Activity.ACS chemical biology · 2023Article
- Substrate Protein Interactions and Methylglyoxal Modifications Reduce the Aggregation Propensity of Human Alpha-A-Crystallin G98R Mutant.Frontiers in molecular biosciences · 2022Article
- Analysis of the data on titration of native and peroxynitrite modified αA- and αB-crystallins by CuData in brief · 2020Article
- Glycation-mediated inter-protein cross-linking is promoted by chaperone-client complexes of α-crystallin: Implications for lens aging and presbyopia.The Journal of biological chemistry · 2020Article
- Connexin hemichannels mediate glutathione transport and protect lens fiber cells from oxidative stress.Journal of cell science · 2018Article
- Small heat shock proteins in ageing and age-related diseases.Cell stress & chaperones · 2017Review
- Effect of methylglyoxal modification on the structure and properties of human small heat shock protein HspB6 (Hsp20).Cell stress & chaperones · 2016Article
- Differential role of arginine mutations on the structure and functions of α-crystallin.Biochimica et biophysica acta · 2016Review
- Therapeutic potential of α-crystallin.Biochimica et biophysica acta · 2016Review
- Characterization of rice small heat shock proteins targeted to different cellular organelles.Cell stress & chaperones · 2015Article
- Role of Subunit Exchange and Electrostatic Interactions on the Chaperone Activity of Mycobacterium leprae HSP18.PloS one · 2015Article
- Acetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin.Biochemistry · 2014Article
- Influence of nonenzymatic posttranslational modifications on constitution, oligomerization and receptor binding of S100A12.PloS one · 2014Article
- Human resistin, a proinflammatory cytokine, shows chaperone-like activity.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Acetylation of lysine 92 improves the chaperone and anti-apoptotic activities of human αB-crystallin.Biochemistry · 2013Article
- Methylglyoxal, obesity, and diabetes.Endocrine · 2013Review
- The combined effect of acetylation and glycation on the chaperone and anti-apoptotic functions of human α-crystallin.Biochimica et biophysica acta · 2013Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Methylglyoxal (MGO) is an α-dicarbonyl compound present ubiquitously in the human body. MGO reacts with arginine residues in proteins and forms adducts such as hydroimidazolone and argpyrimidine in vivo. Previously, we showed that MGO-mediated modification of αA-crystallin increased its chaperone function. We identified MGO-modified arginine residues in αA-crystallin and found that replacing such arginine residues with alanine residues mimicked the effects of MGO on the chaperone function. Arginine 12 (R12) is a conserved amino acid residue in Hsp27 as well as αA- and αB-crystallin. When treated with MGO at or near physiological concentrations (2-10 µM), R12 was modified to hydroimidazolone in all three small heat shock proteins. In this study, we determined the effect of arginine substitution with alanine at position 12 (R12A to mimic MGO modification) on the structure and chaperone function of these proteins. Among the three proteins, the R12A mutation improved the chaperone function of only αA-crystallin. This enhancement in the chaperone function was accompanied by subtle changes in the tertiary structure, which increased the thermodynamic stability of αA-crystallin. This mutation induced the exposure of additional client protein binding sites on αA-crystallin. Altogether, our data suggest that MGO-modification of the conserved R12 in αA-crystallin to hydroimidazolone may play an important role in reducing protein aggregation in the lens during aging and cataract formation.
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