STRUCTURE AND EVOLUTION OF MAMMALIAN RIBOSOMAL-PROTEINS

Citation
Ig. Wool et al., STRUCTURE AND EVOLUTION OF MAMMALIAN RIBOSOMAL-PROTEINS, Biochemistry and cell biology, 73(11-12), 1995, pp. 933-947
Citations number
69
Categorie Soggetti
Biology,"Cell Biology
ISSN journal
08298211
Volume
73
Issue
11-12
Year of publication
1995
Pages
933 - 947
Database
ISI
SICI code
0829-8211(1995)73:11-12<933:SAEOMR>2.0.ZU;2-0
Abstract
Mammalian (rat) ribosomes have 80 proteins; the sequence of amino acid s in 75 have been determined. What has been learned of the structure o f the rat ribosomal proteins is reviewed with particular attention to their evolution and to amino acid sequence motifs. The latter include: clusters of basic or acidic residues; sequence repeats or shared sequ ences; zinc finger domains; bZIP elements; and nuclear localization si gnals. The occurrence and the possible significance of phosphorylated residues and of ubiquitin extensions is noted. The characteristics of the mRNAs that encode the proteins are summarized. The relationship of the rat ribosomal proteins to the proteins in ribosomes from humans, yeast, archaebacteria, and Escherichia coli is collated.