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Abstract:

Trypanosoma cruzi epimastigotes are auxotrophic for polyamines because they are unable to synthesize putrescine de novo. This deficiency is due to the absence of ornithine and arginine decarboxylase genes in the parasite genome. We have been able to obtain transgenic T. cruzi expressing heterologous genes coding for these enzymes. Since arginine decarboxylase normal expression in oat requires a post-translational proteolytic cleavage of an enzyme precursor, we have investigated whether a similar processing occurs inside the transformed protozoa expressing oat arginine decarboxylase or the same enzyme attached to a C-terminal (his)6-tag. We were able to demonstrate that the post-translational processing also takes place inside the transgenic parasites. This cleavage is probably the result of a general proteolytic activity of T. cruzi acting on a protease-sensitive region of the protein. Interestingly, the (his)6-tagged enzyme expressed in the transformed parasites showed considerably increased metabolic stability and catalytic efficiency. © 2008 Elsevier Inc. All rights reserved.

Registro:

Documento: Artículo
Título:Post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in Trypanosoma cruzi epimastigotes
Autor:Serra, M.P.; Senn, A.M.; Algranati, I.D.
Filiación:Fundación Instituto Leloir, IIBBA-CONICET, Facultad de Ciencias Exactas y Naturales, Av. Patricias Argentinas 435, 1405 Buenos Aires, Argentina
Palabras clave:α-difluoromethylarginine; ADC; arginine decarboxylase (EC 4.1.1.9); C-terminal his-tag; carbobenzoxyl-leucinyl-leucinyl-leucinal; DFMA; MG-132; Oat ADC expression; ODC; ornithine decarboxylase (EC 4.1.1.7); Post-translational processing; Protein stability; Trypanosoma (Schizotrypanum) cruzi; arginine decarboxylase; ornithine decarboxylase; article; carboxy terminal sequence; enzyme degradation; enzyme stability; epimastigote; genetic code; heterologous expression; nonhuman; oat; priority journal; protein cleavage; protein expression; protein processing; Trypanosoma cruzi; Amino Acid Sequence; Animals; Avena sativa; Carboxy-Lyases; Gene Expression Regulation, Enzymologic; Kinetics; Molecular Sequence Data; Plasmids; Protein Processing, Post-Translational; Sequence Alignment; Transcription, Genetic; Trypanosoma cruzi; Protozoa; Trypanosoma cruzi
Año:2009
Volumen:122
Número:3
Página de inicio:169
Página de fin:176
DOI: http://dx.doi.org/10.1016/j.exppara.2008.11.007
Título revista:Experimental Parasitology
Título revista abreviado:Exp. Parasitol.
ISSN:00144894
CODEN:EXPAA
CAS:arginine decarboxylase, 9024-77-5; ornithine decarboxylase, 9024-60-6; Carboxy-Lyases, 4.1.1.-; arginine decarboxylase, 4.1.1.19
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00144894_v122_n3_p169_Serra

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Citas:

---------- APA ----------
Serra, M.P., Senn, A.M. & Algranati, I.D. (2009) . Post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in Trypanosoma cruzi epimastigotes. Experimental Parasitology, 122(3), 169-176.
http://dx.doi.org/10.1016/j.exppara.2008.11.007
---------- CHICAGO ----------
Serra, M.P., Senn, A.M., Algranati, I.D. "Post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in Trypanosoma cruzi epimastigotes" . Experimental Parasitology 122, no. 3 (2009) : 169-176.
http://dx.doi.org/10.1016/j.exppara.2008.11.007
---------- MLA ----------
Serra, M.P., Senn, A.M., Algranati, I.D. "Post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in Trypanosoma cruzi epimastigotes" . Experimental Parasitology, vol. 122, no. 3, 2009, pp. 169-176.
http://dx.doi.org/10.1016/j.exppara.2008.11.007
---------- VANCOUVER ----------
Serra, M.P., Senn, A.M., Algranati, I.D. Post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in Trypanosoma cruzi epimastigotes. Exp. Parasitol. 2009;122(3):169-176.
http://dx.doi.org/10.1016/j.exppara.2008.11.007