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Titolo:
Ribosomal protein L5 has a highly twisted concave surface and flexible arms responsible for rRNA binding
Autore:
Nakashima, T; Yao, M; Kawamura, S; Iwasaki, K; Kimura, M; Tanaka, I;
Indirizzi:
Hokkaido Univ, Grad Sch Sci, Div Biol Sci, Sapporo, Hokkaido 0600810, Japan Hokkaido Univ Sapporo Hokkaido Japan 0600810 oro, Hokkaido 0600810, Japan RIKEN, Harima Inst, Div Biocrystallog Technol, Sayo, Hyogo 6795148, Japan RIKEN Sayo Hyogo Japan 6795148 tallog Technol, Sayo, Hyogo 6795148, Japan Kyushu Univ, Fac Agr, Biochem Lab, Fukuoka 8128581, Japan Kyushu Univ Fukuoka Japan 8128581 r, Biochem Lab, Fukuoka 8128581, Japan
Titolo Testata:
RNA-A PUBLICATION OF THE RNA SOCIETY
fascicolo: 5, volume: 7, anno: 2001,
pagine: 692 - 701
SICI:
1355-8382(200105)7:5<692:RPLHAH>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI RIBOSOMES; SITE-DIRECTED MUTAGENESIS; BACILLUS-STEAROTHERMOPHILUS; CRYSTAL-STRUCTURE; ANGSTROM RESOLUTION; NMR STRUCTURE; 5S RNA; L25; COMPLEXES; DOMAIN;
Keywords:
5S rRNA; RNA-binding protein; X-ray structure;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Tanaka, I Hokkaido Univ, Grad Sch Sci, Div Biol Sci, Sapporo, Hokkaido 0600810, Japan Hokkaido Univ Sapporo Hokkaido Japan 0600810 ido 0600810, Japan
Citazione:
T. Nakashima et al., "Ribosomal protein L5 has a highly twisted concave surface and flexible arms responsible for rRNA binding", RNA, 7(5), 2001, pp. 692-701

Abstract

Ribosomal protein L5 is a 5S rRNA binding protein in the large subunit andplays an essential role in the promotion of a particular conformation of 5S rRNA. The crystal structure of the ribosomal protein L5 from Bacillus stearothermophilus has been determined at 1.8 Angstrom resolution. The molecule consists of a five-stranded antiparallel beta -sheet and four alpha -helices, which fold in a way that is topologically similar to the ribonucleoprotein (RNP) domain. The molecular shape and electrostatic representation suggest that the concave surface and loop regions are involved in 5S rRNA binding. To identify amino acid residues responsible for 5S rRNA binding, we made use of Ala-scanning mutagenesis of evolutionarily conserved amino acids occurring in the beta -strands and loop regions. The mutations of Asn37 at the beta1-strand and Gln63 at the loop between helix 2 and beta3-strand as well as that of Phe77 at the tip of the loop structure between the beta2- and beta3-strands caused a significant reduction in 5S rRNA binding. In addition, the mutations of Thr90 on the beta3-strand and Ile141 and Asp144 at the loop between beta4- and beta5-strands moderately reduced the 5S rRNA-binding affinity. Comparison of these results with the more recently analyzed structure of the 50S subunit from Haloarcula marismortui suggests that there are significant differences in the structure at N- and C-terminal regionsand probably in the 5S rRNA binding.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/10/20 alle ore 10:02:57