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Titolo:
Minimal catalytic domain of a group I self-splicing intron RNA
Autore:
Ikawa, Y; Shiraishi, H; Inoue, T;
Indirizzi:
Kyoto Univ, Grad Sch Biostudies, Kyoto 6068502, Japan Kyoto Univ Kyoto Japan 6068502 Grad Sch Biostudies, Kyoto 6068502, Japan
Titolo Testata:
NATURE STRUCTURAL BIOLOGY
fascicolo: 11, volume: 7, anno: 2000,
pagine: 1032 - 1035
SICI:
1072-8368(200011)7:11<1032:MCDOAG>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
TETRAHYMENA RIBOZYME; ACTIVE-SITE; BINDING-SITE; METAL-IONS; TD INTRON; CORE; HELIX;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Inoue, T Kyoto Univ, Grad Sch Biostudies, Kyoto 6068502, Japan Kyoto UnivKyoto Japan 6068502 Biostudies, Kyoto 6068502, Japan
Citazione:
Y. Ikawa et al., "Minimal catalytic domain of a group I self-splicing intron RNA", NAT ST BIOL, 7(11), 2000, pp. 1032-1035

Abstract

The self-splicing intron ribozymes have been regarded as primitive forms of the splicing machinery for eukaryotic pre-mRNAs. The splicing activity ofgroup I self-splicing introns is dependent on an absolutely conserved and exceptionally densely packed core region composed of two helical domains, P3-P7 and P4-P6, that are connected rigidly via base triples. Here we show that a mutant group I intron ribozyme lacking both the P4-P6 domain and the base triples can perform the phosphoester transfer reactions required for splicing at both the 5' and 3' splice sites, demonstrating that the elementsrequired for splicing are concentrated in the stacked helical P3-P7 domain. This finding establishes that the conserved core of the intron consists of two physically and functionally separable components, and we present a model showing the architecture of a prototype of this class of intron and thecourse of its molecular evolution.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 00:48:48