The Journal of Cell Biology, Vol 105, 2095-2102, Copyright © 1987 by The Rockefeller University Press

ARTICLES

Drosophilia spectrin. I. Characterization of the purified protein

R Dubreuil, TJ Byers, D Branton, LS Goldstein and DP Kiehart
Department of Cellular and Developmental Biology, Harvard University, Cambridge, Massachusetts 02138.

We purified a protein from Drosophila S3 tissue culture cells that has many of the diagnostic features of spectrin from vertebrate organisms: (a) The protein consists of two equimolar subunits (Mr = 234 and 226 kD) that can be reversibly cross-linked into a complex composed of equal amounts of the two subunits. (b) Electron microscopy of the native molecule reveals two intertwined, elongated strands with a contour length of 180 nm. (c) Antibodies directed against vertebrate spectrin react with the Drosophila protein and, similarly, antibodies to the Drosophila protein react with vertebrate spectrins. One monoclonal antibody has been found to react with both of the Drosophila subunits and with both subunits of vertebrate brain spectrin. (d) The Drosophila protein exhibits both actin-binding and calcium-dependent calmodulin-binding activities. Based on the above criteria, this protein appears to be a bona fide member of the spectrin family of proteins.
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