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Titolo:
A deteriorated triple-helical scaffold accelerates formation of the Tetrahymena ribozyme active structure
Autore:
Ohki, Y; 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:
FEBS LETTERS
fascicolo: 2-3, volume: 493, anno: 2001,
pagine: 95 - 100
SICI:
0014-5793(20010330)493:2-3<95:ADTSAF>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
COMPARATIVE SEQUENCE-ANALYSIS; GROUP-I RIBOZYME; CATALYTIC DOMAIN; FOLDING PATHWAY; 2 DOMAINS; RNA; INTRONS; SECONDARY; CORE;
Keywords:
group I intron; ribozyme; RNA folding; self-splicing; Tetrahymena;
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. Ohki et al., "A deteriorated triple-helical scaffold accelerates formation of the Tetrahymena ribozyme active structure", FEBS LETTER, 493(2-3), 2001, pp. 95-100

Abstract

The Tetrahymena group I ribozyme requires a hierarchical folding process to form its correct three-dimensional structure. Ribozyme activity depends on the catalytic core consisting of two domains, P4-P6 and P3-P7, connected by a triple-helical scaffold. The folding proceeds in the following order: (i) fast folding of the P4-P6 domain, (ii) slow folding of the P3-P7 domain, and (iii) structure rearrangement to form the active ribozyme structure. The third step is believed to directly determine the conformation of the active catalytic domain, but as yet the precise mechanisms remain to de elucidated. To investigate the folding kinetics of this step, we analyzed mutantribozymes having base substitution(s) in the triple-helical scaffold and found that disruption of the scaffold at A105G results in modest slowing of the P3-P7 folding (1.9-fold) and acceleration of step (iii) by 5.9-fold. These results suggest that disruption or destabilization of the scaffold is anormal component in the formation process of the active structure of the wild type ribozyme. (C) 2001 Published by Elsevier Science B.V. on be half of the Federation of European Biochemical Societies.

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Documento generato il 19/01/20 alle ore 09:24:46