Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Structure of the C-terminal RNA-binding domain of hnRNP D0 (AUF1), its interactions with RNA and DNA, and change in backbone dynamics upon complex formation with DNA
Autore:
Katahira, M; Miyanoiri, Y; Enokizono, Y; Matsuda, G; Nagata, T; Ishikawa, F; Uesugi, S;
Indirizzi:
Grad Sch Environm & Informat Sci, Dept Environm & Nat Sci, Hodogaya Ku, Yokohama, Kanagawa 2408501, Japan Grad Sch Environm & Informat Sci Yokohama Kanagawa Japan 2408501 1, Japan Tokyo Inst Technol, Dept Life Sci, Midori Ku, Yokohama, Kanagawa 226, Japan Tokyo Inst Technol Yokohama Kanagawa Japan 226 ohama, Kanagawa 226, Japan
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 5, volume: 311, anno: 2001,
pagine: 973 - 988
SICI:
0022-2836(20010831)311:5<973:SOTCRD>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR MAGNETIC-RESONANCE; HUMAN U1A PROTEIN; ROTATIONAL DIFFUSION ANISOTROPY; N-15 NMR RELAXATION; DISTANCE GEOMETRY; H-1-NMR SPECTRA; MOLECULAR-DYNAMICS; HETERONUCLEAR NMR; CRYSTAL-STRUCTURE; SEX-LETHAL;
Keywords:
RNA-binding protein; structure; RNA-protein interaction; dynamics; NMR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: Katahira, M Grad Sch Environm & Informat Sci, Dept Environm & Nat Sci, Hodogaya Ku, 79-7 Tokiwadai, Yokohama, Kanagawa 2408501, Japan Grad Sch Environm & Informat Sci 79-7 Tokiwadai Yokohama Kanagawa Japan 2408501
Citazione:
M. Katahira et al., "Structure of the C-terminal RNA-binding domain of hnRNP D0 (AUF1), its interactions with RNA and DNA, and change in backbone dynamics upon complex formation with DNA", J MOL BIOL, 311(5), 2001, pp. 973-988

Abstract

Heterogeneous nuclear ribonucleoprotein (hnRNP) D0 has two ribonucleoprotein (RNP)-type RNA-binding domains (RBDs), each of which can specifically bind to the UUAG-sequence. hnRNP D0 also binds specifically to single-stranded d(TTAGGG)(n), the human telomeric DNA repeat. We have already reported the structure and interactions with RNA of the N-terminal RBD (RBD1). Here, the structure of the C-terminal RBD (RBD2) determined by NMR is presented. It folds into a compact alpha beta structure comprising an antiparallel beta-sheet packed against two alpha -helices, which is characteristic of RNP-type RBDs. In addition to the four beta -strands commonly found in RNP-type RBDs, an extra beta -strand, termed beta4(-), was found just before the fourth beta -strand, yielding a five-stranded beta -sheet. Candidate residues of RBD2 involved in the interactions with RNA were identified by chemical shift perturbation analysis. Perturbation was detected on the beta -sheet side, not on the opposite alpha -helix side, as observed for RBD1. It is notable that the beta4(-) to beta4 region of RBD2 is involved in the interactions in contrast to the case of RBD1. The chemical shift perturbation analysis also showed that RBD2 interacts with DNA in essentially the same way as with RNA. Changes in the backbone dynamics upon complex formation with DNA were examined by means of model free analysis of relaxation data. In free RBD2, the beta4(-) to beta4 region exhibits slow conformational exchange on the milli- to microsecond time scale. The exchange is quenched upon complex formation. The flexibility of free RBD2 may be utilized in the recognition process by allowing different conformational states to be accessed and facilitating induced fit. Additionally, faster flexibility on the nano- to picosecond time scale was observed for loop 3 located between beta2 and beta3 in free RBD2, which is retained by the complex as well. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 22:21:01