Publication details
RNA sequence- and shape-dependent recognition by proteins in the ribonucleoprotein particle
| Authors | |
|---|---|
| Year of publication | 2005 |
| Type | Article in Periodical |
| Magazine / Source | EMBO REPORTS |
| MU Faculty or unit | |
| Citation | |
| Field | Biochemistry |
| Keywords | DOUBLE-STRANDED-RNA; ZINC-FINGER PROTEIN; PRE-RIBOSOMAL-RNA; HUMAN U1A PROTEIN; AU-RICH ELEMENT; BINDING DOMAIN; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; DNA RECOGNITION; |
| Description | At all stages of its life ( from transcription to translation), an RNA transcript interacts with many different RNA-binding proteins. The composition of this supramolecular assembly, known as a ribonucleoprotein particle, is diverse and highly dynamic. RNA-binding proteins control the generation, maturation and lifespan of the RNA transcript and thus regulate and influence the cellular function of the encoded gene. Here, we review our current understanding of protein-RNA recognition mediated by the two most abundant RNA-binding domains (the RNA-recognition motif and the double-stranded RNA-binding motif) plus the zinc-finger motif, the most abundant nucleic-acid-binding domain. In addition, we discuss how not only the sequence but also the shape of the RNA are recognized by these three classes of RNA-binding protein. |