Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La protein
- Details
- Publication Year 2004-04,Volume 11,Issue #4,Page 323-329
- Journal Title
- NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Publication Type
- Journal Article
- Abstract
- The La protein is a conserved component of eukaryotic ribonucleoprotein complexes that binds the 3 poly(U)-rich elements of nascent RNA polymerase III (pol III) transcripts to assist folding and maturation. This specific recognition is mediated by the N-terminal domain (NTD) of La, which comprises a La motif and an RNA recognition motif (RRM). We have determined the solution structures of both domains and show that the La motif adopts an alpha/beta fold that comprises a winged-helix motif elaborated by the insertion of three helices. Chemical shift mapping experiments show that these insertions are involved in RNA interactions. They further delineate a distinct surface patch on each domain containing both basic and aromatic residues that interacts with RNA and accounts for the cooperative binding of short oligonucleotides exhibited by the La NTD.
- Publisher
- NATURE PUBLISHING GROUP
- Keywords
- SITE-MEDIATED TRANSLATION; PRECURSOR TRANSFER-RNAS; SS-B AUTOANTIGEN; CRYSTAL-STRUCTURE; DNA-BINDING; BIOLOGICAL MACROMOLECULES; ANGSTROM RESOLUTION; NMR-SPECTROSCOPY; CHEMICAL-SHIFT; MESSENGER-RNAS
- Publisher's Version
- https://doi.org/10.1038/nsmb747
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2004-04-01 12:00:00