spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Komori, N.
Right arrow Articles by Matsumoto, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Komori, N.
Right arrow Articles by Matsumoto, H.

Journal of Cell Science, Vol 102, Issue 2 191-201, Copyright © 1992 by Company of Biologists

JOURNAL ARTICLES

Drosocrystallin, a major 52 kDa glycoprotein of the Drosophila melanogaster corneal lens. Purification, biochemical characterization, and subcellular localization

N Komori, J Usukura and H Matsumoto
Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City 73190.

We have identified a 52 kDa protein, which is a potent substrate for cholera toxin-dependent ADP-ribosylation, in the compound eye preparation of the fruit fly, Drosophila melanogaster. We find that the 52 kDa protein is a glycoprotein and a Ca2+ binder bearing a high content of leucine, serine and glycine. By microsequencing we determined its 13 N-terminal sequence, AYL*PIDLNQLAK, with the asterisk representing an ambiguous signal. In order to study further the 52 kDa protein we have raised a polyclonal antibody against a synthetic oligopeptide representing the N-terminal 13 residues of the 52 kDa protein. By immunogold labelling with the antibody, the epitopes were localized at the EM level to the laminated corneal lens. The number of the gold particles per microns2 in the electron-dense layer of the corneal lens was 2.5 times higher than that of the electron-lucent layer. The pattern of the 52 kDa protein distribution in the corneal lens suggests that the 52 kDa protein is the major protein component that participates in the pattern formation of the alternate refractive indices of the D. melanogaster corneal lens. An X-ray dispersion analysis in situ revealed that the laminated corneal lens contained a higher concentration of Ca2+, supporting the hypothesis that the 52 kDa protein binds Ca2+ in vivo. To the best of our knowledge, this is the first report that identifies the protein entity of an arthropod corneal lens. We propose to designate this 52 kDa protein drosocrystallin.


This article has been cited by other articles:


Home page
 DevelopmentHome page
J. Blanco, F. Girard, Y. Kamachi, H. Kondoh, and W. J. Gehring
Functional analysis of the chicken {delta}1-crystallin enhancer activity in Drosophila reveals remarkable evolutionary conservation between chicken and fly
Development, April 15, 2005; 132(8): 1895 - 1905.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 1992