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Titolo:
NUCLEAR PRE-TRANSFER-RNA TERMINAL STRUCTURE AND RNASE-P RECOGNITION
Autore:
LEE Y; KINDELBERGER DW; LEE JY; MCCLENNEN S; CHAMBERLAIN J; ENGELKE DR;
Indirizzi:
UNIV MICHIGAN,DEPT BIOL CHEM ANN ARBOR MI 48109 UNIV MICHIGAN,DEPT BIOL CHEM ANN ARBOR MI 48109
Titolo Testata:
RNA
fascicolo: 2, volume: 3, anno: 1997,
pagine: 175 - 185
SICI:
1355-8382(1997)3:2<175:NPTSAR>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
PRECURSOR TRANSFER-RNAS; CATALYTIC M1 RNA; SACCHAROMYCES-CEREVISIAE; RIBONUCLEASE-P; ESCHERICHIA-COLI; RIBONUCLEOPROTEIN ENZYME; CLEAVAGE SPECIFICITY; INTRON MUTATIONS; SEQUENCE CHANGES; POLYMERASE-III;
Keywords:
ENZYME-SUBSTRATE INTERACTION; KINETIC CONSTANTS; NUCLEAR RNASE P; PRE-TRANSFER-RNA STRUCTURE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
53
Recensione:
Indirizzi per estratti:
Citazione:
Y. Lee et al., "NUCLEAR PRE-TRANSFER-RNA TERMINAL STRUCTURE AND RNASE-P RECOGNITION", RNA, 3(2), 1997, pp. 175-185

Abstract

Nuclear pre-tRNA transcripts often contain an extension of the aminoacyl stem formed by base pairing between the 5'-leader and 3'-trailing sequences, but the -1 position preceding the mature 5' end is usually left unpaired. Considering recently proposed tertiary structural models for RNase P RNAs, we hypothesize that the -1 mismatch prevents a strong, coaxially extended aminoacyl stem, which might otherwise sterically interfere with substrate positioning in the RNase P active site. This hypothesis is tested by creating uninterrupted aminoacyl stem extensions in four nuclear tRNA precursors that normally have a mismatched nucleotide at position -1, and comparing their cleavage rates with those of the normal precursors. Determinations of K-m and k(cat) values for a normal and an altered pre-tRNA(SUP53), which exhibits the most subtle structural alteration immediately upstream of the cleavage site, indicate that the mismatch at position -1 is an important structural requirement for both substrate affinity and efficient catalysis (and/orproduct release) by nuclear RNase P. This conclusion is further supported in vivo, where the pre-tRNA(SUP53) mutant precursor lacking the -1 mismatch is shown to accumulate.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 20:47:26