Identification of the factors that interact with NCBP, an 80 kDa nuclear cap binding protein.

It has been shown that the monomethylated cap structure plays important roles in pre-mRNA splicing and nuclear export of RNA. As a candidate for the factor involved in these nuclear events we have previously purified an 80 kDa nuclear cap binding protein (NCBP) from a HeLa cell nuclear extract and ...
isolated its full-length cDNA. In this report, in order to obtain a clue to the cellular functions of NCBP, we attempted to identify a factor(s) that interacts with NCBP. Using the yeast two-hybrid system we isolated three clones from a HeLa cell cDNA library. We designated the proteins encoded by these clones NIPs (NCBP interacting proteins). NIP1 and NIP2 have an RNP consensus-type RNA binding domain, whereas NIP3 contains a unique domain of Arg-Glu or Lys-Glu dipeptide repeats. We also show that NCBP requires NIP1 for binding to the cap structure. Possible roles of NIPs in cap-dependent nuclear processes are discussed.
Mesh Terms:
Amino Acid Sequence, Cloning, Molecular, Dinucleotide Repeats, Hela Cells, Humans, Molecular Sequence Data, Nuclear Cap-Binding Protein Complex, Nuclear Proteins, RNA Cap-Binding Proteins, RNA Caps, RNA, Messenger, RNA-Binding Proteins, Ribonucleoproteins, Sequence Analysis, DNA
Nucleic Acids Res.
Date: Sep. 25, 1995
Download Curated Data For This Publication
9430
Switch View:
  • Interactions 4