Arginine kinase in Phytomonas, a trypanosomatid parasite of plants
Phytomonas are trypanosomatid plant parasites closely related to parasites that cause several human diseases. Little is known about the biology of these organisms including aspects of their metabolism. Arginine kinase (E.C. 2.7.3.3) is a phosphotransferase which catalyzes the interconversion between...
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2011
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10964959_v160_n1_p40_Canepa http://hdl.handle.net/20.500.12110/paper_10964959_v160_n1_p40_Canepa |
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paper:paper_10964959_v160_n1_p40_Canepa2023-06-08T16:07:04Z Arginine kinase in Phytomonas, a trypanosomatid parasite of plants Canepa, Gaspar Exequiel Carrillo, Carolina Pereira, Claudio Alejandro Jatropha macrantha Leishmania Phosphagen Phosphagen kinases Trypanosoma amino acid arginase arginine kinase amino acid sequence article controlled study enzyme activity horizontal gene transfer Leishmania molecular weight nonhuman parasite vector phylogeny Phytomonas priority journal reverse transcription polymerase chain reaction Trypanosoma brucei Trypanosoma cruzi Western blotting Amino Acid Sequence Animals Arginine Kinase Biological Evolution Humans Isoenzymes Molecular Sequence Data Phylogeny Plants Sequence Alignment Trypanosomatina Arthropoda Invertebrata Jatropha Kinetoplastida Phytomonas Trypanosoma Trypanosoma brucei Trypanosoma cruzi Trypanosomatidae Phytomonas are trypanosomatid plant parasites closely related to parasites that cause several human diseases. Little is known about the biology of these organisms including aspects of their metabolism. Arginine kinase (E.C. 2.7.3.3) is a phosphotransferase which catalyzes the interconversion between the phosphagen phosphoarginine and ATP. This enzyme is present in some invertebrates and is a homolog of another widely distributed phosphosphagen kinase, creatine kinase. In this work, a single canonical arginine kinase isoform was detected in Phytomonas Jma by enzymatic activity assays, PCR, and Western Blot. This arginine kinase is very similar to the canonical isoforms found in T. cruzi and T. brucei, presenting about 70% of amino acid sequence identity and a very similar molecular weight (40. kDa). The Phytomonas phosphagen system seems to be very similar to T. cruzi, which has only one isoform, or T. brucei (three isoforms); establishing a difference with other trypanosomatids, such as Leishmania, which completely lacks phosphagen kinases, probably by the presence of the arginine-consuming enzyme, arginase. Finally, phylogenetic analysis suggests that Kinetoplastids' arginine kinase was acquired, during evolution, from the arthropod vectors by horizontal gene transfer. © 2011 Elsevier Inc. Fil:Canepa, G.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Carrillo, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Pereira, C.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2011 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10964959_v160_n1_p40_Canepa http://hdl.handle.net/20.500.12110/paper_10964959_v160_n1_p40_Canepa |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Jatropha macrantha Leishmania Phosphagen Phosphagen kinases Trypanosoma amino acid arginase arginine kinase amino acid sequence article controlled study enzyme activity horizontal gene transfer Leishmania molecular weight nonhuman parasite vector phylogeny Phytomonas priority journal reverse transcription polymerase chain reaction Trypanosoma brucei Trypanosoma cruzi Western blotting Amino Acid Sequence Animals Arginine Kinase Biological Evolution Humans Isoenzymes Molecular Sequence Data Phylogeny Plants Sequence Alignment Trypanosomatina Arthropoda Invertebrata Jatropha Kinetoplastida Phytomonas Trypanosoma Trypanosoma brucei Trypanosoma cruzi Trypanosomatidae |
| spellingShingle |
Jatropha macrantha Leishmania Phosphagen Phosphagen kinases Trypanosoma amino acid arginase arginine kinase amino acid sequence article controlled study enzyme activity horizontal gene transfer Leishmania molecular weight nonhuman parasite vector phylogeny Phytomonas priority journal reverse transcription polymerase chain reaction Trypanosoma brucei Trypanosoma cruzi Western blotting Amino Acid Sequence Animals Arginine Kinase Biological Evolution Humans Isoenzymes Molecular Sequence Data Phylogeny Plants Sequence Alignment Trypanosomatina Arthropoda Invertebrata Jatropha Kinetoplastida Phytomonas Trypanosoma Trypanosoma brucei Trypanosoma cruzi Trypanosomatidae Canepa, Gaspar Exequiel Carrillo, Carolina Pereira, Claudio Alejandro Arginine kinase in Phytomonas, a trypanosomatid parasite of plants |
| topic_facet |
Jatropha macrantha Leishmania Phosphagen Phosphagen kinases Trypanosoma amino acid arginase arginine kinase amino acid sequence article controlled study enzyme activity horizontal gene transfer Leishmania molecular weight nonhuman parasite vector phylogeny Phytomonas priority journal reverse transcription polymerase chain reaction Trypanosoma brucei Trypanosoma cruzi Western blotting Amino Acid Sequence Animals Arginine Kinase Biological Evolution Humans Isoenzymes Molecular Sequence Data Phylogeny Plants Sequence Alignment Trypanosomatina Arthropoda Invertebrata Jatropha Kinetoplastida Phytomonas Trypanosoma Trypanosoma brucei Trypanosoma cruzi Trypanosomatidae |
| description |
Phytomonas are trypanosomatid plant parasites closely related to parasites that cause several human diseases. Little is known about the biology of these organisms including aspects of their metabolism. Arginine kinase (E.C. 2.7.3.3) is a phosphotransferase which catalyzes the interconversion between the phosphagen phosphoarginine and ATP. This enzyme is present in some invertebrates and is a homolog of another widely distributed phosphosphagen kinase, creatine kinase. In this work, a single canonical arginine kinase isoform was detected in Phytomonas Jma by enzymatic activity assays, PCR, and Western Blot. This arginine kinase is very similar to the canonical isoforms found in T. cruzi and T. brucei, presenting about 70% of amino acid sequence identity and a very similar molecular weight (40. kDa). The Phytomonas phosphagen system seems to be very similar to T. cruzi, which has only one isoform, or T. brucei (three isoforms); establishing a difference with other trypanosomatids, such as Leishmania, which completely lacks phosphagen kinases, probably by the presence of the arginine-consuming enzyme, arginase. Finally, phylogenetic analysis suggests that Kinetoplastids' arginine kinase was acquired, during evolution, from the arthropod vectors by horizontal gene transfer. © 2011 Elsevier Inc. |
| author |
Canepa, Gaspar Exequiel Carrillo, Carolina Pereira, Claudio Alejandro |
| author_facet |
Canepa, Gaspar Exequiel Carrillo, Carolina Pereira, Claudio Alejandro |
| author_sort |
Canepa, Gaspar Exequiel |
| title |
Arginine kinase in Phytomonas, a trypanosomatid parasite of plants |
| title_short |
Arginine kinase in Phytomonas, a trypanosomatid parasite of plants |
| title_full |
Arginine kinase in Phytomonas, a trypanosomatid parasite of plants |
| title_fullStr |
Arginine kinase in Phytomonas, a trypanosomatid parasite of plants |
| title_full_unstemmed |
Arginine kinase in Phytomonas, a trypanosomatid parasite of plants |
| title_sort |
arginine kinase in phytomonas, a trypanosomatid parasite of plants |
| publishDate |
2011 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10964959_v160_n1_p40_Canepa http://hdl.handle.net/20.500.12110/paper_10964959_v160_n1_p40_Canepa |
| work_keys_str_mv |
AT canepagasparexequiel argininekinaseinphytomonasatrypanosomatidparasiteofplants AT carrillocarolina argininekinaseinphytomonasatrypanosomatidparasiteofplants AT pereiraclaudioalejandro argininekinaseinphytomonasatrypanosomatidparasiteofplants |
| _version_ |
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