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PMID: 1729676 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Sequence analysis of cytoplasmic mRNA-binding proteins of Xenopus oocytes identifies a family of RNA-binding proteins.

Murray MT, Schiller DL, Franke WW

Abstract

Storage of maternal mRNAs as nontranslated ribonucleoprotein (RNP) complexes is an adaptive strategy in various vertebrate and invertebrate oocytes, for rapid translational recruitment during embryonic development. Previously, we showed that Xenopus laevis oocytes have a soluble cytoplasmic pool of mRNA-binding proteins and particles competent for messenger RNP assembly in vitro. Here we report the isolation of cDNAs for the most abundant messenger RNPs, the 54- and 56-kDa polypeptide (p54/p56) components of the approximately 6S mRNA-binding particle, from an ovarian expression library. The nucleotide sequence of p56 cDNA is almost identical to that recently reported for the putative Xenopus transcription factor FRG Y2. p54 and p56 are highly homologous and are smaller than expected by SDS/PAGE (36 kDa and 37 kDa) due to anomalous electrophoretic mobility. They lack the "RNP consensus motif" but contain four arginine-rich "basic/aromatic islands" that are similar to the RNA-binding domain of bacteriophage mRNA antiterminator proteins and of tat protein of human immunodeficiency virus. The basic/aromatic regions and a second conspicuous 100-amino acid "domain C" of p54 and p56 are conserved in the following DNA-binding proteins: human proteins dpbA, dpbB, and YB-1, rat protein EFIA, and Xenopus protein FRG Y1, all reported to bind to DNA; domain C is homologous to the major Escherichia coli cold-stress-response protein reportedly involved in translational control. Antibodies raised against a peptide of domain C have identified similar proteins in Xenopus somatic cells and in some mammalian cells and tissues. We conclude that p54 and p56 define a family of RNA-binding proteins, at least some of which may be involved in translational regulation.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Cloning, Molecular Cytoplasm/chemistry DNA/genetics Molecular Sequence Data Molecular Weight Multigene Family Oocytes/chemistry RNA, Messenger/genetics,metabolism RNA-Binding Proteins/chemistry,genetics,metabolism Sequence Alignment Xenopus laevis
Chemicals
RNA, Messenger RNA-Binding Proteins DNA
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Murray M T
Division of Membrane Biology and Biochemistry, German Cancer Research Center, Heidelberg.
Schiller D L
Franke W W
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1992-01-01
Pages
11-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC48164
Subset
IM
Databases
GENBANK
M80257
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