Abstract
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.
Original language | American English |
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Pages (from-to) | 797-809 |
Number of pages | 13 |
Journal | Journal of cell science |
Volume | 103 |
Issue number | 3 |
State | Published - Nov 1992 |
ASJC Scopus subject areas
- Cell Biology
Keywords
- RNA-binding sequences
- Sea urchin egg
- Vesicles