Mol Cell Biol. 1989 December; 9(12): 5281-5288
Developmental expression and 5S rRNA-binding activity of Xenopus laevis ribosomal protein L5.
W M Wormington
Department of Biology, University of Virginia, Charlottesville 22901.
ABSTRACT
Ribosomal protein L5 binds specifically to 5S rRNA to form a complex that is a precursor to 60S subunit assembly in vivo. Analyses in yeast cells, mammalian cells, and Xenopus embryos have shown that the accumulation of L5 is not coordinated with the expression of other ribosomal proteins. In this study, the primary structure and developmental expression of Xenopus ribosomal protein L5 were examined to determine the basis for its distinct regulation. These analyses showed that L5 expression could either coincide with 5S rRNA synthesis and ribosome assembly or be controlled independently of these events at different stages of Xenopus development. L5 synthesis during oogenesis was uncoupled from the accumulation of 5S rRNa but coincided with subunit assembly. In early embryos, the inefficient translation of L5 mRNA resulted in the accumulation of a stable L5-5S rRNA complex before ribosome assembly at later stages of development. Additional results demonstrated that L5 protein synthesized in vitro bound specifically to 5S rRNA.
Mol Cell Biol. 1989 December; 9(12): 5281-5288
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Copyright © 1989 by the American Society for Microbiology. All rights reserved.