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Titolo:
THE INTERFERON-INDUCED 67-KDA GUANYLATE-BINDING PROTEIN (HGBP1) IS A GTPASE THAT CONVERTS GTP TO GMP
Autore:
SCHWEMMLE M; STAEHELI P;
Indirizzi:
UNIV FREIBURG,INST MIKROBIOL & HYG,VIROL ABT,HERMANN HERDER STR 11 D-79008 FREIBURG GERMANY UNIV FREIBURG,INST MIKROBIOL & HYG,VIROL ABT,HERMANN HERDER STR 11 D-79008 FREIBURG GERMANY
Titolo Testata:
The Journal of biological chemistry
fascicolo: 15, volume: 269, anno: 1994,
pagine: 11299 - 11305
SICI:
0021-9258(1994)269:15<11299:TI6GP(>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOUSE MX1 PROTEIN; CELLULAR PROTEINS; DOMAIN; MOTIF; P21; MECHANISM; MEMBRANE; VIRUS; GDP;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
M. Schwemmle e P. Staeheli, "THE INTERFERON-INDUCED 67-KDA GUANYLATE-BINDING PROTEIN (HGBP1) IS A GTPASE THAT CONVERTS GTP TO GMP", The Journal of biological chemistry, 269(15), 1994, pp. 11299-11305

Abstract

hGBP1 is an interferon-induced 67-kDa protein of human cells that readily binds to agarose-immobilized GTP, GDP, and GMP but not to other nucleotides. We cloned hGBP1 cDNA into a histidine-tagging vector, produced recombinant hGBP1 with 6 extra histidine residues at its N terminus in Escherichia coli, and purified this protein to near homogeneity from bacterial lysates. Purified hGBP1 hydrolyzed radiolabeled GTP butfailed to hydrolyze ATP, UTP, or CTP at significant rates. Unexpectedly, the principal product of the GTP hydrolysis reaction was GMP rather than GDP. Although significant amounts of GDP were produced when thereaction was performed at 15-degrees-C, GDP could not serve as substrate or as inhibitor of hGBP1. hGBP1 lacked guanylate cyclase and guanylyltransferase activity. Degradation of GTP to GMP most likely occurred via two consecutive cleavages of single phosphate groups, because pyrophosphate was not a reaction product, and because hGBP1 failed to hydrolyze GTPgammaS. In vitro modification assays with radiolabeled mevalonic acid and farnesyl pyrophosphate showed that the CaaX motif at the C terminus of hGBP1 functions as an isoprenylation signal. Thus, hGBP1 is a GTPase with novel biochemical properties that may be membrane-associated in eukaryotic cells.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/20 alle ore 16:14:12