Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a component of apobec-1 editosome.

ApoB mRNA editing is mediated by an editosome complex with apobec-1 as its catalytic component. By yeast two-hybrid cloning using apobec-1 as bait we identified a 69.6-kDa RNA binding protein, GRY-RBP, that contains 3 RNA-recognition motifs (RRMs) as a novel apobec-1 associating protein. GRY-RBP may be an alternatively spliced species ...
of NASP1, a protein of known function. GRY-RBP was shown to bind to apobec-1, the catalytic component of apoB mRNA editosome, in vivo and in vitro. Immunodepletion using a monospecific rabbit antibody abolished editing in apobec-1 expressing HepG2 S-100 extracts. GRY-RBD interacted with apobec-1 through its C-terminus. It contains three RRM (RNA recognition motifs) domains that are homologous to those found in human ACF (apobec-1 complementation factor). Phylogeny analysis of the RRM domain-containing proteins indicates that GRY-RBP clusters with hnRNP-R, ACF, and ABBP-1 (another apobec-1 binding protein). In addition to its involvement with apobec-1 editosome, the suggested cellular functions of GRY-RBD and its structural homologues include RNA transport and RNA secondary structure stabilization.
Mesh Terms:
Amino Acid Motifs, Amino Acid Sequence, Antibodies, Cloning, Molecular, Cytidine Deaminase, Heterogeneous-Nuclear Ribonucleoproteins, Humans, Macromolecular Substances, Molecular Sequence Data, Phylogeny, Protein Structure, Tertiary, RNA Editing, RNA, Messenger, RNA-Binding Proteins, Sequence Homology, Amino Acid, Tissue Distribution, Tumor Cells, Cultured, Two-Hybrid System Techniques
Biochem. Biophys. Res. Commun.
Date: Apr. 13, 2001
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