Identification of the factors that interact with NCBP, an 80 kDa nuclear cap binding protein.
AUTOR(ES)
Kataoka, N
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=307259Documentos Relacionados
- Cloning of a complementary DNA encoding an 80 kilodalton nuclear cap binding protein.
- DNA binding properties of a 110 kDa nucleolar protein.
- Identification of an integral membrane 80 kDa protein of Saccharomyces cerevisiae induced in response to dehydration
- The TIP1 gene of Saccharomyces cerevisiae encodes an 80 kDa cytoplasmic protein that interacts with the cytoplasmic domain of Sec20p.
- PNRC2 is a 16 kDa coactivator that interacts with nuclear receptors through an SH3-binding motif