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Titolo:
Molecular mass, stoichiometry, and assembly of 20 S particles
Autore:
Wimmer, C; Hohl, TM; Hughes, CA; Muller, SA; Sollner, TH; Engel, A; Rothman, JE;
Indirizzi:
Mem Sloan Kettering Canc Ctr, New York, NY 10021 USA Mem Sloan Kettering Canc Ctr New York NY USA 10021 New York, NY 10021 USA Univ Basel, Bioctr, Maurice E Muller Inst High Resolut Electron M, CH-4056Basel, Switzerland Univ Basel Basel Switzerland CH-4056 ectron M, CH-4056Basel, Switzerland
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 31, volume: 276, anno: 2001,
pagine: 29091 - 29097
SICI:
0021-9258(20010803)276:31<29091:MMSAAO>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
SENSITIVE FUSION PROTEIN; NSF-ATTACHMENT PROTEINS; TRANSMISSION ELECTRON-MICROSCOPY; INTEGRAL MEMBRANE-PROTEIN; OLIGOMERIC MATRIX PROTEIN; ALPHA-HELICAL BUNDLE; SNARE COMPLEX; CRYSTAL-STRUCTURE; VESICULAR TRANSPORT; IN-VITRO;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
63
Recensione:
Indirizzi per estratti:
Indirizzo: Wimmer, C Basel Inst Immunol, Grenzacherstr 487, CH-4005 Basel, Switzerland Basel Inst Immunol Grenzacherstr 487 Basel Switzerland CH-4005
Citazione:
C. Wimmer et al., "Molecular mass, stoichiometry, and assembly of 20 S particles", J BIOL CHEM, 276(31), 2001, pp. 29091-29097

Abstract

N-Ethylmaleimide-sensitive factor (NSF), soluble NSF attachment proteins (SNAPs), and SNAP receptor (neuronal SNARE) complexes form 20 S particles with a mass of 788 +/- 122 kDa as judged by scanning transmission electron microscopy. A single NSF hexamer and three alpha SNAP monomers reside within a 20 S particle as determined by quantitative amino acid analysis. In orderto study the binding of aSNAP and NSF in solution, to define their bindingdomains, and to specify the role of oligomerization in their interaction, we fused domains of aSNAP and NSF to oligomerization modules derived from thrombospondin-1, a trimer, and cartilage oligomeric matrix protein, a pentamer, respectively. Binding studies with these fusion proteins reproduced the interaction of aSNAP and NSF N domains in the absence of the hexamerization domain of NSF (D2). Trimeric aSNAP (or its C-terminal half) is sufficient to recruit NSF even in the absence of SNARE complexes. Furthermore, pentameric NSF N domains are able to bind aSNAP in complex with SNARES, whereas monomeric N domains do not. Our results demonstrate that the oligomerization of both NSF N domains and aSNAP provides a critical driving force for their interaction and the assembly of 20 S particles.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 03:05:26