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THE PLANT CELL, Vol 7, Issue 4 391-406, Copyright © 1995 by American Society of Plant Biologists
The Tobacco Homolog of Mammalian Calreticulin Is Present in Protein Complexes in Vivo
J. Denecke, L. E. Carlsson, S. Vidal, A. S. Hoglund, B. Ek, M. J. van Zeijl, KMC. Sinjorgo and E. T. Palva
Swedish University of Agricultural Sciences, Uppsala Genetic Center, Department of Molecular Genetics, Box 7010, Uppsala, Sweden
The analysis of protein sorting signals responsible for the retention of
reticuloplasmins (RPLs), a group of soluble proteins that reside in the
lumen of the endoplasmic reticulum (ER), has revealed a structural
similarity between mammalian and plant ER retention signals. We present
evidence that the corresponding epitope is conserved in a vast family of
soluble ER resident proteins. Microsequences of RPL60 and RPL90, two
abundant members of this family, show high sequence similarity with
mammalian calreticulin and endoplasmin. RPL60/calreticulin cofractionates
and costains with the lumenal binding protein (BiP). Both proteins were
detected in the nuclear envelope and the ER, and in mitotic cells in
association with the spindle apparatus and the phragmoplast.
Immunoprecipitation of proteins from in vivo-labeled cells demonstrated
that RPL60/calreticulin is associated with other polypeptides in a stress-
and ATP-dependent fashion. RPL60/calreticulin transcript levels increased
rapidly in abundance during the proliferation of the secretory apparatus
and the onset of hydrolase secretion in gibberellic acid-treated barley
aleurone cells. This induction profile is identical to that of the
well-characterized ER chaperones BiP and endoplasmin. However, expression
patterns in response to different stress conditions as well as
tissue-specific expression patterns indicate that these genes are
differentially regulated and may not act in concert.
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