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Titolo:
MGATP BINDING TO THE NUCLEOTIDE-BINDING DOMAINS OF THE EUKARYOTIC CYTOPLASMIC CHAPERONIN INDUCES CONFORMATIONAL-CHANGES IN THE PUTATIVE SUBSTRATE-BINDING DOMAINS
Autore:
SZPIKOWSKA BK; SWIDEREK KM; SHERMAN MA; MAS MT;
Indirizzi:
CITY HOPE NATL MED CTR,BECKMAN RES INST,DIV BIOL,PHYS BIOCHEM SECT DUARTE CA 91010 CITY HOPE NATL MED CTR,BECKMAN RES INST,DIV BIOL,PHYS BIOCHEM SECT DUARTE CA 91010 CITY HOPE NATL MED CTR,BECKMAN RES INST,DIV IMMUNOL DUARTE CA 91010
Titolo Testata:
Protein science
fascicolo: 7, volume: 7, anno: 1998,
pagine: 1524 - 1530
SICI:
0961-8368(1998)7:7<1524:MBTTND>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
TANDEM MASS-SPECTROMETRY; T-COMPLEX POLYPEPTIDE-1; CYTOSOLIC CHAPERONIN; PEPTIDE MIXTURES; CONTAINING TCP-1; RING COMPLEX; BETA-ACTIN; GROEL; SUBUNITS; IDENTIFICATION;
Keywords:
CCT; LIMITED PROTEOLYSIS; LONG-RANGE CONFORMATIONAL CHANGES; MASS SPECTROMETRY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
29
Recensione:
Indirizzi per estratti:
Citazione:
B.K. Szpikowska et al., "MGATP BINDING TO THE NUCLEOTIDE-BINDING DOMAINS OF THE EUKARYOTIC CYTOPLASMIC CHAPERONIN INDUCES CONFORMATIONAL-CHANGES IN THE PUTATIVE SUBSTRATE-BINDING DOMAINS", Protein science, 7(7), 1998, pp. 1524-1530

Abstract

The eukaryotic cytosolic chaperonins are large heterooligomeric complexes with a cylindrical shape, resembling that of the homooligomeric bacterial counterpart, GroEL. In analogy to GroEL, changes in shape of the cytosolic chaperonin have been detected in the presence of MgATP using electron microscopy but, in contrast to the nucleotide-induced conformational changes in GroEL, no details are available about the specific nature of these changes. The present study identifies the structural regions of the cytosolic chaperonin that undergo conformational changes when MgATP binds to the nucleotide binding domains. It is shown that limited proteolysis with trypsin in the absence of MgATP cleaves each of the eight subunits approximately in half, generating two fragments of similar to 30 kDa. Using mass spectrometry (MS) and N-terminalsequence analysis, the cleavage is found to occur in a narrow span ofthe amino acid sequence, corresponding to the peptide binding regionsof GroEL and to the helical protrusion, recently identified in the structure of the substrate binding domain of the archeal group II chaperonin. This proteolytic cleavage is prevented by MgATP but not by ATP in the absence of magnesium, ATP analogs (MgATP gamma S and MgAMP-PNP) or MgADP. These results suggest that, in analogy to GroEL, binding of MgATP to the nucleotide binding domains of the cytosolic chaperonin induces long range conformational changes in the polypeptide binding domains. It is postulated that despite their different subunit composition and substrate specificity, group I and group II chaperonins may share similar, functionally-important, conformational changes. Additional conformational changes are Likely to involve a flexible helix-loop-helix motif, which is characteristic for all group II chaperonins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 07:17:19