scholarly journals Leishmania amazonensis: Biological and biochemical characterization of ecto-nucleoside triphosphate diphosphohydrolase activities

2006 ◽  
Vol 114 (1) ◽  
pp. 16-25 ◽  
Author(s):  
Carla M. Pinheiro ◽  
Erica S. Martins-Duarte ◽  
Rodrigo B. Ferraro ◽  
André Luíz Fonseca de Souza ◽  
Marta T. Gomes ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Leishmania Amazonensis ◽  
Nucleoside Triphosphate ◽  
Nucleoside Triphosphate Diphosphohydrolase

Trypanosoma brucei brucei: Biochemical characterization of ecto-nucleoside triphosphate diphosphohydrolase activities

2007 ◽  
Vol 115 (4) ◽  
pp. 315-323 ◽  
Author(s):  
Milane de Souza Leite ◽  
Rachel Thomaz ◽  
Fábio Vasconcelos Fonseca ◽  
Rogério Panizzutti ◽  
Anibal E. Vercesi ◽  
...  
Keyword(s):  
Trypanosoma Brucei ◽  
Biochemical Characterization ◽  
Nucleoside Triphosphate ◽  
Trypanosoma Brucei Brucei ◽  
Nucleoside Triphosphate Diphosphohydrolase

Kinetic and biochemical characterization of Trypanosoma evansi nucleoside triphosphate diphosphohydrolase

2015 ◽  
Vol 153 ◽  
pp. 98-104 ◽  
Author(s):  
Paulo Henrique Exterchoter Weiss ◽  
Franciane Batista ◽  
Glauber Wagner ◽  
Maria de Lourdes Borba Magalhães ◽  
Luiz Claudio Miletti
Keyword(s):  
Biochemical Characterization ◽  
Trypanosoma Evansi ◽  
Nucleoside Triphosphate ◽  
Nucleoside Triphosphate Diphosphohydrolase

scholarly journals Trypanosoma cruzi nucleoside triphosphate diphosphohydrolase 1 (TcNTPDase-1) biochemical characterization, immunolocalization and possible role in host cell adhesion

Acta Tropica ◽  
2014 ◽  
Vol 130 ◽  
pp. 140-147 ◽  
Author(s):  
Christiane Mariotini-Moura ◽  
Matheus Silva e Bastos ◽  
Felipe Freitas de Castro ◽  
Mellina Lanna Trindade ◽  
Raphael de Souza Vasconcellos ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Trypanosoma Cruzi ◽  
Host Cell ◽  
Biochemical Characterization ◽  
Nucleoside Triphosphate ◽  
Nucleoside Triphosphate Diphosphohydrolase

Cloning and Characterization of Mouse Nucleoside Triphosphate Diphosphohydrolase-8†,‡

Biochemistry ◽  
2004 ◽  
Vol 43 (18) ◽  
pp. 5511-5519 ◽  
Author(s):  
François Bigonnesse ◽  
Sébastien A. Lévesque ◽  
Filip Kukulski ◽  
Joanna Lecka ◽  
Simon C. Robson ◽  
...  
Keyword(s):  
Nucleoside Triphosphate ◽  
Nucleoside Triphosphate Diphosphohydrolase

scholarly journals Identification and characterization of mutations in the UPF1 gene that affect nonsense suppression and the formation of the Upf protein complex but not mRNA turnover.

1996 ◽  
Vol 16 (10) ◽  
pp. 5491-5506 ◽  
Author(s):  
Y Weng ◽  
K Czaplinski ◽  
S W Peltz
Keyword(s):  
Mrna Decay ◽  
Rna Binding ◽  
Biochemical Characterization ◽  
Translation Termination ◽  
Nonsense Suppression ◽  
Nucleoside Triphosphate ◽  
Rich Region ◽  
Amino Terminal ◽  
Nonsense Mediated Mrna Decay

To understand the relationship between translation and mRNA decay, we have been studying how premature translation termination accelerates the degradation of mRNAs. In the yeast Saccharomyces cerevisiae, the Upf1 protein (Upf1p), which contains a cysteine- and histidine-rich region and nucleoside triphosphate hydrolysis and helicase motifs, was shown to be a trans-acting factor in this decay pathway. A UPF1 gene disruption results in the stabilization of nonsense-containing mRNAs and leads to a nonsense suppression phenotype. Biochemical analysis of the wild-type Upf1p demonstrated that it has RNA-dependent ATPase, RNA helicase, and RNA binding activities. In the work described in the accompanying paper (Y. Weng, K. Czaplinski, and S. W. Peltz, Mol. Cell. Biol. 16:5477-5490, 1996) mutations in the helicase region of Upf1p that inactivated its mRNA decay function but prevented suppression of leu2-2 and tyr7-1 nonsense alleles are identified. On the basis of these results, we suggested that Upf1p is a multifunctional protein involved in modulating mRNA decay and translation termination at nonsense codons. If this is true, we predict that UPF1 mutations with the converse phenotype should be identified. In this report, we describe the identification and biochemical characterization of mutations in the amino-terminal cysteine- and histidine-rich region of Upf1p that have normal nonsense-mediated mRNA decay activities but are able to suppress leu2-2 and tyr7-1 nonsense alleles. Biochemical characterization of these mutant proteins demonstrated that they have altered RNA binding properties. Furthermore, using the two-hybrid system, we characterized the Upf1p-Upf2p interactions and demonstrated that Upf2p interacts with Upf3p. Mutations in the cysteine- and histidine-rich region of Upf1p abolish Upf1p-Upf2p interaction. On the basis of these results, the role of the Upf complex in nonsense-mediated mRNA decay and nonsense suppression is discussed.

scholarly journals Biochemical characterization of Arabidopsis APYRASE family reveals their roles in regulating endomembrane NDP/NMP homoeostasis

2015 ◽  
Vol 472 (1) ◽  
pp. 43-54 ◽  
Author(s):  
Tsan-Yu Chiu ◽  
Jeemeng Lao ◽  
Bianca Manalansan ◽  
Dominique Loqué ◽  
Stanley J. Roux ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Nucleoside Triphosphate ◽  
Nucleoside Diphosphatase ◽  
Nucleoside Triphosphatase

The seven apyrase enzymes from Arabidopsis localize to the plant endomembrane. Our analyses indicate that five members (AtAPY1, 2, 4, 5 and 6) exhibit lumenal NDPase (nucleoside diphosphatase) activities whereas AtAPY3 has NTPase (nucleoside triphosphatase) activity. AtAPY7 displayed no nucleoside triphosphate diphosphohydrolases (NTPDase) activity.

Distribution, cloning, and characterization of porcine nucleoside triphosphate diphosphohydrolase-1

2000 ◽  
Vol 267 (13) ◽  
pp. 4106-4114 ◽  
Author(s):  
Raf Lemmens ◽  
Luc Vanduffel ◽  
Agnes Kittel ◽  
Adrien R. Beaudoin ◽  
Ouhida Benrezzak ◽  
...  
Keyword(s):  
Nucleoside Triphosphate ◽  
Nucleoside Triphosphate Diphosphohydrolase
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