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Titolo:
DOMAINS MEDIATING INTRAMOLECULAR FOLDING AND OLIGOMERIZATION OF MXA GTPASE
Autore:
SCHUMACHER B; STAEHELI P;
Indirizzi:
UNIV FREIBURG,DEPT VIROL,INST MED MIKROBIOL & HYG,ABT VIROL,HERMANN HERDER STR 11 D-79008 FREIBURG GERMANY UNIV FREIBURG,DEPT VIROL,INST MED MIKROBIOL & HYG,ABT VIROL D-79008 FREIBURG GERMANY
Titolo Testata:
The Journal of biological chemistry
fascicolo: 43, volume: 273, anno: 1998,
pagine: 28365 - 28370
SICI:
0021-9258(1998)273:43<28365:DMIFAO>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
INDUCED HUMAN PROTEIN; INFLUENZA-VIRUS; ANTIVIRAL ACTIVITY; INTERFERON; INHIBITION; BINDING; RESISTANCE; HOMOLOGY; MICE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
26
Recensione:
Indirizzi per estratti:
Citazione:
B. Schumacher e P. Staeheli, "DOMAINS MEDIATING INTRAMOLECULAR FOLDING AND OLIGOMERIZATION OF MXA GTPASE", The Journal of biological chemistry, 273(43), 1998, pp. 28365-28370

Abstract

MxA is an interferon-induced GTPase of human cells that inhibits the multiplication of several RNA viruses by a still poorly understood mechanism. Previous biochemical studies indicated that the C terminus of MxA folds back to form a functional GTP-binding pocket, and that an internal fragment contains a domain required for oligomerization. Using the yeast two-hybrid system, we have now mapped these domains. MxA sequences located downstream of amino acid 564 were found to strongly interact with an internal domain that includes amino acids 372 to 540, This interaction was abolished by mutating phenylalanine 382 or leucine 612, which is part, of a leucine zipper motif. Neither the C-terminal nor the internal MxA fragments formed homo-oligomers. Using a mammalian nuclear transport assay that can detect protein-protein interactions, we further found that full-length MxA forms complexes with MxA fragments that include amino acids 372 to 540. This interaction was not observed when phenylalanine 382 was exchanged for alanine or arginine. Furthermore, interaction of two full-length MxA molecules occurred only if at least one of them carried a functional C-terminal leucine zippermotif, These results suggest that C-terminal back-folding and oligomerization are two alternative outcomes of the same type of interaction between the C-terminal and the internal domains of MxA. Intramolecularinteraction is believed to result in the formation of MxA monomers, whereas intermolecular interaction may induce the formation of large MxA oligomers.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/01/20 alle ore 09:49:36