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Titolo:
IN-VIVO ZIPPERING OF INNER AND OUTER MITOCHONDRIAL-MEMBRANES BY A STABLE TRANSLOCATION INTERMEDIATE
Autore:
SCHULKE N; SEPURI NBV; PAIN D;
Indirizzi:
UNIV PENN,SCH MED,DEPT PHYSIOL,D403 RICHARDS BLDG,3700 HAMILTON WALK PHILADELPHIA PA 19104 UNIV PENN,SCH MED,DEPT PHYSIOL PHILADELPHIA PA 19104
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 14, volume: 94, anno: 1997,
pagine: 7314 - 7319
SICI:
0027-8424(1997)94:14<7314:IZOIAO>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN IMPORT MACHINERY; PURIFIED PRECURSOR PROTEIN; CONTACT SITES; YEAST MITOCHONDRIA; DYNAMIC INTERACTION; IDENTIFICATION; HSP70; RECEPTOR; ENVELOPE; PATHWAY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
N. Schulke et al., "IN-VIVO ZIPPERING OF INNER AND OUTER MITOCHONDRIAL-MEMBRANES BY A STABLE TRANSLOCATION INTERMEDIATE", Proceedings of the National Academy of Sciences of the United Statesof America, 94(14), 1997, pp. 7314-7319

Abstract

It was previously assumed that the import of cytoplasmically synthesized precursor proteins into mitochondria occurs through a single structure spanning both outer and inner membranes at contact sites. Based on recent findings, however, the two membranes appear to contain independent translocation elements that reversibly cooperate during protein import. This feature makes it difficult to generate a means of isolating a fully integrated and functional translocation complex. To study these independent translocases in vitro and in vivo, we have constructed a chimeric protein consisting of an N-terminal authentic mitochondrial precursor (delta(1)-pyrroline-5-carboxylate dehydrogenase) linked, through glutathione S-transferase, to IgG binding domains derived fromstaphylococcal protein A. This construct becomes trapped en route to the matrix, spanning both outer and inner membranes in such a way thatthe entire signal-less delta(1)-pyrroline-5-carboxylate dehydrogenasemoiety reaches the matrix, while only the folded protein A domain remains outside. During in vivo import of this precursor, outer and innermembranes of yeast mitochondria become progressively ''zippered'' together, forming long stretches of close contact. Using this novel intermediate, the outer and inner mitochondrial membrane channels, which normally interact only transiently, can be tightly joined (both in vitroand in vivo), forming a stable association. This suggests a method for isolating the functional translocation complex as a single entity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 10:17:49