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Protein Science (2004), 13:678-686. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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Laser light-scattering evidence for an altered association of {beta}B1-crystallin deamidated in the connecting peptide

Michael J. Harms1, Philip A. Wilmarth1, Deborah M. Kapfer1, Eric A. Steel2, Larry L. David1, Hans Peter Bächinger2 and Kirsten J. Lampi1

1 Oregon Health & Science University, Portland, Oregon 97239, USA
2 Shriners Hospital for Children, Portland, Oregon, 97239, USA

(RECEIVED September 9, 2003; FINAL REVISION November 21, 2003; ACCEPTED December 2, 2003)



Abstract

Deamidation is a prevalent modification of crystallin proteins in the vertebrate lens. The effect of specific sites of deamidation on crystallin stability in vivo is not known. Using mass spectrometry, a previously unreported deamidation in {beta}B1-crystallin was identified at Gln146. Another deamidation was investigated at Asn157. It was determined that whole soluble {beta}B1 contained 13%–17% deamidation at Gln146 and Asn157. Static and quasi-elastic laser light scattering, circular dichroism, and heat aggregation studies were used to explore the structure and associative properties of recombinantly expressed wild-type (wt) {beta}B1 and the deamidated {beta}B1 mutants, Q146E and N157D. Dimer formation occurred for wt {beta}B1, Q146E, and N157D in a concentration-dependent manner, but only Q146E showed formation of higher ordered oligomers at the concentrations studied. Deamidation at Gln146, but not Asn157, led to an increased tendency of {beta}B1 to aggregate upon heating. We conclude that deamidation creates unique effects depending upon where the deamidation is introduced in the crystallin structure.

Keywords: lens crystallins; deamidation; cataracts; oligomer assembly; laser light-scattering; mass spectrometry

Reprint requests to: Kirsten J. Lampi, Integrative Biosciences, School of Dentistry, Oregon Health and Science University, 611 SW Campus Drive, Portland, OR 97239, USA; e-mail: lampik{at}ohsu.edu; fax: (503) 494-8918.

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03427504.


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