A novel vesicle-associated protein (vap-1) in sea urchin eggs containing multiple rna-binding consensus sequences
Author(s) -
N R Barton,
Edward M. Bonder,
D J Fishkind,
R H Warren,
M M Pratt
Publication year - 1992
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.103.3.797
Subject(s) - biology , rna , strongylocentrotus purpuratus , rna binding protein , consensus sequence , sea urchin , microbiology and biotechnology , biochemistry , peptide sequence , gene
We have identified a novel high molecular weight, vesicle-associated protein (VAP-1) in the eggs of the sea urchin Strongylocentrotus purpuratus. Biochemical fractionation and immunofluorescence analysis of unfertilized eggs indicate that VAP-1 is a peripheral membrane protein associated with microsomal membrane fractions. Sequence analysis of partial VAP-1 cDNA clones reveals that the protein contains at least four RNA-binding consensus sequences. The RNA-binding sequences are separated by several glycine rich domains and this organization, RNA-binding domains separated by glycine rich sequences, is common to several RNA-binding proteins including the heterogeneous ribonuclear protein A1 and nucleolin. The characteristics of VAP-1 suggest that the protein may function as a multidomain RNA-binding protein. The possibility that VAP-1 may play a role in nuclear RNA processing is also discussed.
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