| First Author | Tamada H | Year | 2002 |
| Journal | Biochem Biophys Res Commun | Volume | 297 |
| Issue | 1 | Pages | 96-104 |
| PubMed ID | 12220514 | Mgi Jnum | J:78809 |
| Mgi Id | MGI:2386312 | Doi | 10.1016/s0006-291x(02)02132-0 |
| Citation | Tamada H, et al. (2002) cDNA cloning and characterization of Drb1, a new member of RRM-type neural RNA-binding protein. Biochem Biophys Res Commun 297(1):96 |
| abstractText | Neural RNA recognition motif (RRM)-type RNA-binding proteins play essential roles in neural development. To search for a new member of neural RRM-type RNA-binding protein, we screened rat cerebral expression library with polyclonal antibody against consensus RRM sequences. We have cloned and characterized a rat cDNA that belongs to RRM-type RNA-binding protein family, which we designate as drb1. Orthologs of drb1 exist in human and mouse. The predicted amino acid sequence reveals an open reading frame of 476 residues with a corresponding molecular mass of 53kDa and consists of four RNA-binding domains. drb1 gene is specifically expressed in fetal (E12, E16) rat brain and gradually reduced during development. In situ hybridization demonstrated neuron-specific signals in fetal rat brain. RNA-binding assay indicated that human Drb1 protein possesses binding preference on poly(C)RNA. These results indicate that Drb1 is a new member of neural RNA-binding proteins, which expresses under spatiotemporal control. |
