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Volume 270, Number 29, Issue of July 21, pp. 17215-17220, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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Conversion from Oligomers to Tetramers Enhances Autophosphorylation by Lens A-Crystallin
SPECIFICITY BETWEEN A- AND B-CRYSTALLIN SUBUNITS

(Received for publication, December 23, 1994)

From the  (1)Laboratory of Molecular and Developmental Biology, NEI, National Institutes of Health, Bethesda, Maryland 20892, the (2)Jules Stein Eye Institute, UCLA School of Medicine, Los Angeles, California 90024, and the (3)Department of Biochemistry, University of Nijmegen, 6525 EK Nijmegen, The Netherlands

Previously we showed that -crystallins are autophosphorylated (Kantorow, M., and Piatigorsky, J.(1994) Proc. Natl. Acad. Sci. U. S. A. 91, 3112-3116). Here we report that addition of 1% deoxycholate converted A-crystallin aggregates into 80-kDa tetramers which were 10-fold more active for autophosphorylation. Circular dichroism (CD) spectra of -crystallin revealed little or no change in secondary and tertiary structures in 1% deoxycholate. A2D, a truncated form of bovine A that exists as a tetramer, was as active for autophosphorylation in the absence of deoxycholate as intact A was in the presence of deoxycholate. At least one serine between amino acids 131 and 145 of bovine A was autophosphorylated in peptide mapping experiments. Chicken A-crystallin, which lacks the Ser-122 cAMP-dependent kinase site of bovine A, was also autophosphorylated in the presence of deoxycholate. In contrast to A-crystallin, autophosphorylation by B-crystallin was not activated by deoxycholate despite its conversion to a tetrameric form, and B was also more efficiently phosphorylated by cAMP-dependent kinase than A. These data suggest metabolic differences between the -crystallin subunits that may be related to specific expression of A in the lens and ubiquitous expression of B in numerous normal and diseased tissues.

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