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Titolo:
Conformational changes induced in the Saccharomyces cerevisiae GTPase-associated rRNA by ribosomal stalk components and a translocation inhibitor
Autore:
Briones, C; Ballesta, JPG;
Indirizzi:
CSIC, Ctr Biol Mol Severo Ochoa, Madrid 28049, Spain CSIC Madrid Spain 28049 , Ctr Biol Mol Severo Ochoa, Madrid 28049, Spain Univ Autonoma Madrid, Madrid 28049, Spain Univ Autonoma Madrid Madrid Spain 28049 noma Madrid, Madrid 28049, Spain
Titolo Testata:
NUCLEIC ACIDS RESEARCH
fascicolo: 22, volume: 28, anno: 2000,
pagine: 4497 - 4505
SICI:
0305-1048(20001115)28:22<4497:CCIITS>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
FUNGAL PROTEIN-SYNTHESIS; ELONGATION-FACTOR-G; ESCHERICHIA-COLI; ACIDIC PHOSPHOPROTEINS; EUKARYOTIC ELONGATION-FACTOR-2; SELECTIVE-INHIBITION; RNA STRUCTURES; 23S RNA; EF-G; COMPLEX;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
55
Recensione:
Indirizzi per estratti:
Indirizzo: Ballesta, JPG CSIC, Ctr Biol Mol Severo Ochoa, Canto Blanco, Madrid 28049,Spain CSIC Canto Blanco Madrid Spain 28049 o, Madrid 28049, Spain
Citazione:
C. Briones e J.P.G. Ballesta, "Conformational changes induced in the Saccharomyces cerevisiae GTPase-associated rRNA by ribosomal stalk components and a translocation inhibitor", NUCL ACID R, 28(22), 2000, pp. 4497-4505

Abstract

The yeast ribosomal GTPase associated center is made of parts of the 26S rRNA domains II and VI, and a number of proteins including P0, P1 alpha, P1 beta, P2 alpha, P2 beta and L12, Mapping of the rRNA neighborhood of the proteins was performed by footprinting in ribosomes from yeast strains lacking different GTPase components, The absence of protein PO dramatically increases the sensitivity of the defective ribosome to degradation hampering theRNA footprinting, In ribosomes lacking the P1/P2 complex, protection of a number of nucleotides is detected around positions 840, 880, 1100, 1220-1280 and 1350 in domain II as well as in several positions in the domain VI alpha -sarcin region, The protection pattern resembles the one reported for the interaction of elongation factors in bacterial systems. The results exclude a direct interaction of these proteins with the rRNA and are compatiblewith an increase in the ribosome affinity for EF-2 in the absence of the acidic P proteins, Interestingly, a sordarin derivative inhibitor of EF-2 causes an opposite effect, increasing the reactivity in positions protected by the absence of P1/P2, Similarly, a deficiency in protein L12 exposes nucleotides G1235, G1242, A1262, A1269, A1270 and A1272 to chemical modification, thus situating the protein binding site in the most conserved part of the 26S rRNA, equivalent to the bacterial protein L11 binding site.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 00:26:29