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Published July 1, 1987 | Published
Journal Article Open

Regulated expression of multiple chicken erythroid membrane skeletal protein 4.1 variants is governed by differential RNA processing and translational control

Abstract

Protein 4.1 is an extrinsic membrane protein that facilitates the interaction of spectrin and actin in the erythroid membrane skeleton and exists as several structurally related polypeptides in chickens. The ratio of protein 4.1 variants is developmentally regulated during terminal differentiation of chicken erythroid and lenticular cells. To examine the mechanisms by which multiple chicken protein 4.1 variants are differentially expressed, we have isolated cDNA clones specific for chicken erythroid protein 4.1. We show that a single protein 4.1 gene gives rise to multiple 6.6-kilobase mRNAs by differential RNA processing. Furthermore, the ratios of protein 4.1 mRNAs change during chicken embryonic erythropoiesis. We observe a quantitative difference in variant ratios when protein 4.1 is synthesized in vivo or in a rabbit reticulocyte lysate in vitro. Our results show that the expression of multiple protein 4.1 polypeptides is regulated at the levels of translation and RNA processing.

Additional Information

© 1987 by the National Academy of Sciences. Communicated by Melvin I. Simon, March 23, 1987. We thank Drs. Bruce Granger, Barbara Wold, and John Cox for helpful discussions during the course of this study. This work was supported by grants from the National Institutes of Health, the National Science Foundation, and Muscular Dystrophy Association of America. J.N. was also supported by a Gordon Ross Foundation Fellowship; J.H.S. by a training grant from the National Institutes of Health (T32 GM07616), and R.T.M. by an American Cancer Society postdoctoral fellowship. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

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