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Titolo:
SMALL-ANGLE NEUTRON-SCATTERING ANALYSIS OF THERMAL-STABILITY OF 23S RIBOSOMAL-RNA AND THE INTACT 50S SUBUNITS OF SULFOLOBUS-SOLFATARICUS
Autore:
BRIGANTI G; GIORDANO R; LONDEI P; PEDONE F;
Indirizzi:
UNIV ROMA LA SAPIENZA,DEPT PHYS,INFM,PA MORO 2 I-00185 ROME ITALY UNIV ROMA LA SAPIENZA,DEPT MOL BIOL I-00185 ROME ITALY UNIV ROMA LA SAPIENZA,DEP BIOPATOL UMANA I-00185 ROME ITALY UNIV MESSINA,DEPT PHYS,INFM I-98100 MESSINA ME ITALY UNIV BARI,FAC MED,IST BIOL GEN BARI ITALY
Titolo Testata:
Biochimica et biophysica acta (G). General subjects
fascicolo: 2, volume: 1379, anno: 1998,
pagine: 297 - 301
SICI:
0304-4165(1998)1379:2<297:SNAOTO>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
ARCHAEBACTERIUM SULFOLOBUS; RIBOSOMAL-SUBUNITS; FEATURES;
Keywords:
TEMPERATURE EVOLUTION; GROWTH TEMPERATURE; (50S 23S S-SOLFATARICUS);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
6
Recensione:
Indirizzi per estratti:
Citazione:
G. Briganti et al., "SMALL-ANGLE NEUTRON-SCATTERING ANALYSIS OF THERMAL-STABILITY OF 23S RIBOSOMAL-RNA AND THE INTACT 50S SUBUNITS OF SULFOLOBUS-SOLFATARICUS", Biochimica et biophysica acta (G). General subjects, 1379(2), 1998, pp. 297-301

Abstract

The ribosomes of the extremely thermophilic archaebacterium, Sulfolobus solfataricus, are very resistant to thermal denaturation (optimal growth temperature 87 degrees C), remaining essentially intact up to above 90 degrees C, However, the separate ribosomal components (rRNA andr-proteins) are less thermally stable than the ribosome as a whole, indicating that the mode of interaction of all of the components withinthe ribonucleoprotein particle play an essential role in determining thermal stability, To get some insight into the structural features ofthe thermophilic ribosome, we performed small angle neutron scattering (SANS) measurements at various temperatures on Sulfolobus solfataricus intact large ribosomal subunits (50S) and deproteinated large ribosomal subunit RNA (23S). Even if the scattering profiles suggest the presence of supramolecular aggregates in all of the samples and at all of the investigated temperatures, the measured form factors indicated for both samples that, at temperatures above 70 degrees C, the suspended particles underwent a structural rearrangement. This finding is likely to reflect single particles' properties, since S. solfataricus ribosomes are known to be biologically activated only above 60 degrees C, and there are indications that such activation requires a conformational rearrangement of the particle, A remarkable superimposition of the percentage variation of the volume from neutron scattering and of the absorbancy increment with respect to temperature supports this view. (C) 1998 Elsevier Science B.V.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 15:31:12