| First Author | Hirose Y | Year | 2008 |
| Journal | Biochem Biophys Res Commun | Volume | 365 |
| Issue | 1 | Pages | 62-8 |
| PubMed ID | 17971306 | Mgi Jnum | J:128459 |
| Mgi Id | MGI:3767137 | Doi | 10.1016/j.bbrc.2007.10.117 |
| Citation | Hirose Y, et al. (2008) Mouse nucleolin binds to 4.5S RNAh, a small noncoding RNA. Biochem Biophys Res Commun 365(1):62-8 |
| abstractText | 4.5S RNAh is a rodent-specific small noncoding RNA that exhibits extensive homology to the B1 short interspersed element. Although 4.5S RNAh is known to associate with cellular poly(A)-terminated RNAs and retroviral genomic RNAs, its function remains unclear. In this study, we analyzed 4.5S RNAh-binding proteins in mouse nuclear extracts using gel mobility shift and RNA-protein UV cross-linking assays. We found that at least nine distinct polypeptides (p170, p110, p93, p70, p48, p40, p34, p20, and p16.5) specifically interacted with 4.5S RNAhin vitro. Using anti-La antibody, p48 was identified as mouse La protein. To identify the other 4.5S RNAh-binding proteins, we performed expression cloning from a mouse cDNA library and obtained cDNA clones derived from nucleolin mRNA. We identified p110 as nucleolin using nucleolin-specific antibodies. UV cross-linking analysis using various deletion mutants of nucleolin indicated that the third of four tandem RNA recognition motifs is a major determinant for 4.5S RNAh recognition. Immunoprecipitation of nucleolin from the subcellular fractions of mouse cell extracts revealed that a portion of the endogenous 4.5S RNAh was associated with nucleolin and that this complex was located in both the nucleoplasm and nucleolus. |
