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Titolo:
EFFECTS OF ANTISENSE DNA AGAINST THE ALPHA-SARCIN STEM-LOOP STRUCTUREOF THE RIBOSOMAL 23S RIBOSOMAL-RNA
Autore:
MEYER HA; TRIANAALONSO F; SPAHN CMT; TWARDOWSKI T; SOBKIEWICZ A; NIERHAUS KH;
Indirizzi:
MAX PLANCK INST MOL GENET,AG RIBOSOMEN,IHNESTR 73 D-14195 BERLIN GERMANY MAX PLANCK INST MOL GENET,AG RIBOSOMEN D-14195 BERLIN GERMANY POLISH ACAD SCI,INST BIOORGAN CHEM PL-61704 POZNAN POLAND
Titolo Testata:
Nucleic acids research
fascicolo: 20, volume: 24, anno: 1996,
pagine: 3996 - 4002
SICI:
0305-1048(1996)24:20<3996:EOADAT>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI RIBOSOMES; TRANSFER-RNA BINDING; ELONGATION-FACTORS; RICIN LOOP; SITE; CLEAVAGE; REGION; OLIGONUCLEOTIDES; TRANSLATION; TOPOGRAPHY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
H.A. Meyer et al., "EFFECTS OF ANTISENSE DNA AGAINST THE ALPHA-SARCIN STEM-LOOP STRUCTUREOF THE RIBOSOMAL 23S RIBOSOMAL-RNA", Nucleic acids research, 24(20), 1996, pp. 3996-4002

Abstract

Antisense DNAs complementary against various sequences of the alpha-sarcin domain (C2640-G2674) of 235 rRNA from Escherichia coli were hybridized to naked 235 rRNA as well as to 70S ribosomes. Saturation levels of up to 0.4 per 70S ribosome were found, the identical fraction wassusceptible to the attack of the RNase alpha-sarcin. The hybridization was specific as demonstrated with RNase H digestion, sequencing the resulting fragments and blockage of the action of alpha-sarcin. The RNase alpha-sarcin seems to approach its cleavage site from the 3' half of the loop of the alpha-sarcin domain. Hybridization is efficiently achieved at 37 degrees C and can extend at least into the 3' strand of the stem of the alpha-sarcin domain. However, the inhibition of alpha-sarcin activity is observed at 30 degrees C but not at 37 degrees C. For a significant inhibition of poly(Phe) synthesis the temperature hadto be lowered to 25 degrees C. The results imply that the alpha-sarcin domain changes its conformation during protein synthesis and that the conformational changes may include a melting of the stem of the alpha-sarcin domain.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 08:55:13