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Titolo:
Functional role of Chaperonin protein complexes
Autore:
Briganti, G; Giordano, R; Londei, P; Valle, F;
Indirizzi:
Univ La Sapienza, INFM, Unita Romal, Dept Phys, I-00185 Rome, Italy Univ La Sapienza Rome Italy I-00185 omal, Dept Phys, I-00185 Rome, Italy Univ Messina, INFM, Dept Phys, Messina, Italy Univ Messina Messina Italy niv Messina, INFM, Dept Phys, Messina, Italy Univ Bari, Ist Biol Gen, I-70121 Bari, Italy Univ Bari Bari Italy I-70121 niv Bari, Ist Biol Gen, I-70121 Bari, Italy Univ Rome, Dept Cellular Biotechnol & Hematol, Rome, Italy Univ Rome Rome Italy e, Dept Cellular Biotechnol & Hematol, Rome, Italy
Titolo Testata:
PHYSICA B
, volume: 276, anno: 2000,
pagine: 516 - 517
SICI:
0921-4526(200003)276:<516:FROCPC>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
ARCHAEON SULFOLOBUS-SOLFATARICUS;
Keywords:
proteins; small-angle neutron scattering;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
5
Recensione:
Indirizzi per estratti:
Indirizzo: Briganti, G Univ La Sapienza, INFM, Unita Romal, Dept Phys, PA Moro 5, I-00185 Rome, Italy Univ La Sapienza PA Moro 5 Rome Italy I-00185 185 Rome, Italy
Citazione:
G. Briganti et al., "Functional role of Chaperonin protein complexes", PHYSICA B, 276, 2000, pp. 516-517

Abstract

The chaperonins are high-molecular weight protein complexes present in allliving cells; they are thought to participate in the folding or refolding of cellular proteins and may also have a function in RNA metabolism. Recently, it has been reported that the chaperonin of thermophilic archeon Sulfolobus solfataricus interacts with the 16S ribosomal RNA and participates in the early stages of its maturation. By means of contrast variation SANS we demonstrate that the native S. solfataricus chaperonin is complexed with a nucleic acid molecule of about 1600 nucleotides, which becomes detached from the protein mojety in the presence of ATP. Treatment with ATP also provokes a conformational change in the protein complex, compacting its structureand closing its central hole. The result lends support to the hypothesis that Sulfolobus chaperonin participates in ribosomal RNA maturation and ribosome assembly. (C) 2000 Elsevier Science B.V. All rights reserved.

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Documento generato il 30/09/20 alle ore 09:38:57