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TcArf1: a Trypanosoma cruzi ADP-ribosylation factor
Parasitology Research, 2003Arfs (ADP-ribosylation factors) are conserved GTP-binding proteins involved in the control of coatomers assembling in budding vesicles in the eukaryotic secretory pathway and during some endocytic events. Here, we describe the gene for an Arf-homologue from the unicellular kinetoplastid parasite Trypanosoma cruzi, named TcArf1.
Alexandre, de Sá-Freire +5 more
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Activation of toxin ADP-ribosyltransferases by eukaryotic ADP-ribosylation factors
Molecular and Cellular Biochemistry, 1999ADP-ribosylation factors (ARFs) are members of a multigene family of 20-kDa guanine nucleotide-binding proteins that are regulatory components in several pathways of intracellular vesicular trafficking. The relatively small (approximately 180-amino acids) ARF proteins interact with a variety of molecules (in addition to GTP/GDP, of course).
J, Moss, M, Vaughan
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Assays of ADP-Ribosylation factor Function
2002ADP-ribosylation factors (ARFs) comprise a family of 20-kDa GTPases first identified as the protein cofactor required for the ADP ribosylation of the G s α protein, catalyzed by the A 1 subunits of the bacterial toxins cholera toxin (CT) and Escherichia colt heat-labile toxin (UF).
Jun, Kuai, Richard A, Kahn
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Cellular ADP-ribosylation of Elongation Factor 2
Molecular and Cellular Biochemistry, 1994A cellular ADP-ribosyltransferase activity has been found in a variety of animals and tissues. The enzyme transfers ADP-ribose from NAD to elongation factor 2, inactivating the factor and thus inhibiting in vitro protein synthesis. Although, the mechanism of action of the cellular enzyme appears similar to diphtheria toxin and Pseudomonas exotoxin A ...
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1994
Abstract Cloned ARF cDNA predicts a protein with a glycine at this position. Each of the three human ARF cDNAs hARF11314 (accession number P10947), hARF315 (accession number P16587), and hARF4,3,15 (accession numbers P18085, P21371) encode proteins of 180 or 181 amino acids with predicted molecular masses of 21-22 kDa.
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Abstract Cloned ARF cDNA predicts a protein with a glycine at this position. Each of the three human ARF cDNAs hARF11314 (accession number P10947), hARF315 (accession number P16587), and hARF4,3,15 (accession numbers P18085, P21371) encode proteins of 180 or 181 amino acids with predicted molecular masses of 21-22 kDa.
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Molecular Characterization of ADP-Ribosylation Factors
1993Cholera toxin (CT) is largely responsible for the pathogenesis of cholera, a devastating diarrheal disease characterized by marked abnormalities in fluid and electrolyte flux (Carpenter 1980; Finkelstein 1973; Kelly 1986). The toxin, a product of Vibrio cholerae, is an oligomeric protein composed of one A subunit (CTA) of about 29kDa and five B ...
J. Moss, M. Vaughan
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ADP-ribosylation Factors Protein Activators of Cholera Toxin
1993Publisher Summary The toxins alter the activity of the guanine nucleotide-binding proteins (G proteins) by catalyzing the transfer of the ADP-ribose moiety of NAD to a critical amino acid in the a subunit. This ADP-ribosylation reaction results in either activation (e.g., cholera toxin, E.
J, Moss, M, Vaughan
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ADP-ribosylation factors (Arfs)
1999Abstract AP180 is an abundant neurone-specific clathrin-associated phosphoprotein, which supports in vitro the assembly of clathrin triskelia into a homogeneous population of cage-like structures. This function appears to be regulated by inositol polyphosphates. Proteins related to AP180 are also expressed in non-neuronal cells.
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ADP-Ribosylation Factor-1 Is Sensitive to N-Ethylmaleimide
Journal of Biochemistry, 1998The treatment of normal rat kidney cells with N-ethylmaleimide caused the release of beta-COP, a component of coatomer, from the Golgi apparatus without causing disassembly of the organelle. The release of beta-COP, which was not due to depolymerization of microtubules, was markedly blocked by the activation of GTP-binding proteins by aluminum fluoride
T, Yamaguchi +5 more
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Archaebacterial elongation factor is ADP-ribosylated by diphtheria toxin
Nature, 1980Archaebacteria have been defined as a 'third primary kingdom' of cells in addition to the urkaryotes and the eubacteria. While the latter two correspond approximately to the conventional categories eukaryotes and prokaryotes respectively, the Archaebacteria have up to now comprised four groups of microorganisms: the methanogenic bacteria, the extremely
M, Kessel, F, Klink
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