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Protein Science, Vol 7, Issue 6 1451-1457, Copyright © 1998 by Cold Spring Harbor Laboratory Press

ARTICLE

In vivo acetylation identified at lysine 70 of human lens {alpha}A-crystallin

P. P. LIN, R. C. BARRY, D. L. SMITH and J. B. SMITH
Current address: MDS Harris Laboratories, Inc., Lincoln, Nebraska 68502.

Posttranslational modification of protein lysyl residues that change the net charge of the molecule may alter the protein conformation. Such modifications are of particular significance among lens proteins, because conformational changes are associated with the development of cataract. A previously unidentified acetylated form of {alpha}A-crystallin has been isolated from the water-soluble portion of human lenses. The {alpha}A-crystallins were fractionated by anion exchange HPLC into seven peaks, each containing more than one form of {alpha}A-crystallin. The previously reported deamidated and phosphorylated forms were identified by their molecular masses, determined by electrospray ionization mass spectrometry. In addition to these modifications, approximately 5% of {alpha}A-crystallin had a modification that decreased the charge by one and increased the molecular mass by 42 u. This modification, identified as acetylation, was located uniquely at Lys 70. Like any modification that alters the surface charge, acetylation may affect protein conformation and intermolecular interactions, thereby altering the solubility or chaperone properties of {alpha}A-crystallin. Acetylation of lysine 70 is potentially significant since it is located in a region that has been implicated in the chaperone activity of {alpha}A-crystallin.
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