Post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in Trypanosoma cruzi epimastigotes
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...
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2009
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| LEADER | 13379caa a22013457a 4500 | ||
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| 001 | PAPER-8677 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203829.0 | ||
| 008 | 190411s2009 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-67349162534 | |
| 024 | 7 | |2 cas |a arginine decarboxylase, 9024-77-5; ornithine decarboxylase, 9024-60-6; Carboxy-Lyases, 4.1.1.-; arginine decarboxylase, 4.1.1.19 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a EXPAA | ||
| 100 | 1 | |a Serra, M.P. | |
| 245 | 1 | 0 | |a Post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in Trypanosoma cruzi epimastigotes |
| 260 | |c 2009 | ||
| 270 | 1 | 0 | |m Algranati, I.D.; Fundación Instituto Leloir, IIBBA-CONICET, Facultad de Ciencias Exactas y Naturales, Av. Patricias Argentinas 435, 1405 Buenos Aires, Argentina; email: ialgranati@leloir.org.ar |
| 506 | |2 openaire |e Política editorial | ||
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| 504 | |a Malmberg, R.L., Cellino, M.L., Arginine decarboxylase of oats is activated by enzymatic cleavage into two polypeptides (1994) Journal of Biological Chemistry, 269, pp. 2703-2706 | ||
| 504 | |a Malmberg, R.L., Smith, K.E., Bell, E., Cellino, M.L., Arginine decarboxylase of oats is clipped from a precursor into two polypeptides found in the soluble enzyme (1992) Plant Physiology, 100, pp. 146-152 | ||
| 504 | |a Martínez-Calvillo, S., López, I., Hernández, R., pRIBOTEX expression vector: a pTEX derivative for a rapid selection of Trypanosoma cruzi transfectants (1997) Gene, 199, pp. 71-76 | ||
| 504 | |a Nasizadeh, S., Jeppsson, A., Persson, L., Proteasomal degradation of a trypanosomal ornithine decarboxylase (2003) Cellular Physiology and Biochemistry, 13, pp. 321-328 | ||
| 504 | |a Pegg, A.E., Regulation of ornithine decarboxylase (2006) Journal of Biological Chemistry, 281, pp. 14529-14538 | ||
| 504 | |a Persson, L., Jeppsson, A., Nasizadeh, S., Turnover of trypanosomal ornithine decarboxylases (2003) Biochemical Society Transactions, 31, pp. 411-414 | ||
| 504 | |a Santos, A.L., Abreu, C.M., Alviano, C.S., Soares, R.M., Use of proteolytic enzymes as an additional tool for trypanosomatid identification (2005) Parasitology, 130, pp. 79-88 | ||
| 504 | |a Segel, I.H., (1993) Enzyme Kinetics, , John Wiley, New York | ||
| 504 | |a Segura, E.L., Subias, E., Esteva, M., Cabeza Meckert, P., Brozina, A., Laguens, R.P., Características de infectividad de tres poblaciones de cultivo de Trypanosoma cruzi (1980) Medicina (Buenos Aires), 40, pp. 97-102 | ||
| 504 | |a Serra, M.P., Carrillo, C., González, N.S., Algranati, I.D., Modulation of oat arginine decarboxylase gene expression and genome organization in transgenic Trypanosoma cruzi epimastigotes (2006) FEBS Journal, 273, pp. 628-637 | ||
| 504 | |a Shah, R., Akella, R., Goldsmith, E.J., Phillips, M.A., X-ray structure of Paramecium bursaria Chlorella virus arginine decarboxylase: insight into the structural basis for substrate specificity (2007) Biochemistry, 46, pp. 2831-2841 | ||
| 504 | |a Steglich, C., Schaeffer, S.W., The ornithine decarboxylase gene of Trypanosoma brucei: evidence for horizontal gene transfer from a vertebrade source (2006) Infection, Genetics and Evolution, 6, pp. 205-219 | ||
| 504 | |a Uzurean, P., Felu, C., De Muylder, G., Pays, E., Vanhamme, L., G418, phleomycin and hygromycin selection of recombinant Trypanosoma brucei parasites refractory to long-term in vitro culture (2007) Molecular and Biochemical Parasitology, 154, pp. 90-94 | ||
| 504 | |a Zhang, M., Pickart, C.M., Coffino, P., Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate (2003) EMBO Journal, 22, pp. 1488-1496 | ||
| 520 | 3 | |a 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. |l eng | |
| 536 | |a Detalles de la financiación: Universidad de Buenos Aires | ||
| 536 | |a Detalles de la financiación: We appreciate the collaboration of Dr. N.S. González who carried out the experiment of in vitro synthesis of radioactive ADC and the subsequent processing of the translation product. We also thank Drs. S.H. Goldemberg and M. Juri Ayoub for helpful discussions and Edith Trejo and Carlos Zadikian for technical assistance. This work was partially supported by the University of Buenos Aires. | ||
| 593 | |a Fundación Instituto Leloir, IIBBA-CONICET, Facultad de Ciencias Exactas y Naturales, Av. Patricias Argentinas 435, 1405 Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a Α-DIFLUOROMETHYLARGININE |
| 690 | 1 | 0 | |a ARGININE DECARBOXYLASE (EC 4.1.1.9) |
| 690 | 1 | 0 | |a C-TERMINAL HIS-TAG |
| 690 | 1 | 0 | |a CARBOBENZOXYL-LEUCINYL-LEUCINYL-LEUCINAL |
| 690 | 1 | 0 | |a DFMA |
| 690 | 1 | 0 | |a MG-132 |
| 690 | 1 | 0 | |a OAT ADC EXPRESSION |
| 690 | 1 | 0 | |a ODC |
| 690 | 1 | 0 | |a ORNITHINE DECARBOXYLASE (EC 4.1.1.7) |
| 690 | 1 | 0 | |a POST-TRANSLATIONAL PROCESSING |
| 690 | 1 | 0 | |a PROTEIN STABILITY |
| 690 | 1 | 0 | |a TRYPANOSOMA (SCHIZOTRYPANUM) CRUZI |
| 690 | 1 | 0 | |a ARGININE DECARBOXYLASE |
| 690 | 1 | 0 | |a ORNITHINE DECARBOXYLASE |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a CARBOXY TERMINAL SEQUENCE |
| 690 | 1 | 0 | |a ENZYME DEGRADATION |
| 690 | 1 | 0 | |a ENZYME STABILITY |
| 690 | 1 | 0 | |a EPIMASTIGOTE |
| 690 | 1 | 0 | |a GENETIC CODE |
| 690 | 1 | 0 | |a HETEROLOGOUS EXPRESSION |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a OAT |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a PROTEIN CLEAVAGE |
| 690 | 1 | 0 | |a PROTEIN EXPRESSION |
| 690 | 1 | 0 | |a PROTEIN PROCESSING |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 690 | 1 | 0 | |a AMINO ACID SEQUENCE |
| 690 | 1 | 0 | |a ANIMALS |
| 690 | 1 | 0 | |a AVENA SATIVA |
| 690 | 1 | 0 | |a CARBOXY-LYASES |
| 690 | 1 | 0 | |a GENE EXPRESSION REGULATION, ENZYMOLOGIC |
| 690 | 1 | 0 | |a KINETICS |
| 690 | 1 | 0 | |a MOLECULAR SEQUENCE DATA |
| 690 | 1 | 0 | |a PLASMIDS |
| 690 | 1 | 0 | |a PROTEIN PROCESSING, POST-TRANSLATIONAL |
| 690 | 1 | 0 | |a SEQUENCE ALIGNMENT |
| 690 | 1 | 0 | |a TRANSCRIPTION, GENETIC |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 690 | 1 | 0 | |a PROTOZOA |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 650 | 1 | 7 | |2 spines |a ADC |
| 700 | 1 | |a Senn, A.M. | |
| 700 | 1 | |a Algranati, I.D. | |
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