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Biochemistry ; 58(9): 1260-1274, 2019 03 05.
Article in English | MEDLINE | ID: mdl-30758948

ABSTRACT

Acylation of lysine residues is a common post-translational modification of cellular proteins. Here, we show that lysine succinylation, a type of acylation, occurs in human lens proteins. All of the major crystallins exhibited Nε-succinyllysine (SuccK) residues. Quantification of SuccK in human lens proteins (from donors between the ages of 20 and 73 years) by LC-MS/MS showed a range between 1.2 and 14.3 pmol/mg lens protein. The total SuccK levels were slightly reduced in aged lenses (age > 60 years) relative to young lenses (age < 30 years). Immunohistochemical analyses revealed that SuccK was present in epithelium and fiber cells. Western blotting and immunoprecipitation experiments revealed that SuccK is particularly prominent in αB-crystallin, and succinylation in vitro revealed that αB-crystallin is more prone to succinylation than αA-crystallin. Mass spectrometric analyses showed succinylation at K72, K90, K92, K166, K175, and potentially K174 in human lens αB-crystallin. We detected succinylation at K72, K82, K90, K92, K103, K121, K150, K166, K175, and potentially K174 by mass spectrometry in mildly succinylated αB-crystallin. Mild succinylation improved the chaperone activity of αB-crystallin along with minor perturbation in tertiary and quaternary structure of the protein. These observations imply that succinylation is beneficial to αB-crystallin by improving its chaperone activity with only mild conformational alterations.


Subject(s)
Lens, Crystalline/metabolism , Lysine/analysis , Lysine/metabolism , alpha-Crystallin B Chain/metabolism , Adult , Age Factors , Aged , Chromatography, Liquid , Circular Dichroism , Crystallins/metabolism , Gain of Function Mutation , Humans , Lens, Crystalline/chemistry , Middle Aged , Molecular Chaperones/chemistry , Molecular Chaperones/genetics , Molecular Chaperones/metabolism , Protein Conformation , Succinates/metabolism , Tandem Mass Spectrometry , alpha-Crystallin B Chain/chemistry , alpha-Crystallin B Chain/genetics
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