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Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La protein


Alfano, C; Sanfelice, D; Babon, J; Kelly, G; Jacks, A; Curry, S; Conte, MR
2004-04
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Journal Article
11
4
323-329
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.
NATURE PUBLISHING GROUP
SITE-MEDIATED TRANSLATION; PRECURSOR TRANSFER-RNAS; SS-B AUTOANTIGEN; CRYSTAL-STRUCTURE; DNA-BINDING; BIOLOGICAL MACROMOLECULES; ANGSTROM RESOLUTION; NMR-SPECTROSCOPY; CHEMICAL-SHIFT; MESSENGER-RNAS
10.1038/nsmb747
Refer to copyright notice on published article.

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Creation Date 2004-04-01 12:00:00