Characterization of a novel translational inhibitor from Leishmania mexicana promastigotes.

An inhibitory activity blocking protein synthesis elongation in several eukaryotic systems has been detected in Leishmania mexicana extracts. This factor, which competes with aminoacylation of tRNA and also affects the subsequent polymerization step, is a strong inhibitor of polypeptide synthesis in...

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Detalles Bibliográficos
Autores principales:	Fastame, I.G., Algranati, I.D.
Formato:	JOUR
Materias:	protein synthesis inhibitor protozoal RNA animal article genetics isolation and purification Leishmania mexicana metabolism protein synthesis Animals Protein Biosynthesis Protein Synthesis Inhibitors RNA, Protozoan
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_01455680_v44_n3_p475_Fastame
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_01455680_v44_n3_p475_Fastame
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spelling	todo:paper_01455680_v44_n3_p475_Fastame2023-10-03T15:00:01Z Characterization of a novel translational inhibitor from Leishmania mexicana promastigotes. Fastame, I.G. Algranati, I.D. protein synthesis inhibitor protozoal RNA animal article genetics isolation and purification Leishmania mexicana metabolism protein synthesis Animals Leishmania mexicana Protein Biosynthesis Protein Synthesis Inhibitors RNA, Protozoan An inhibitory activity blocking protein synthesis elongation in several eukaryotic systems has been detected in Leishmania mexicana extracts. This factor, which competes with aminoacylation of tRNA and also affects the subsequent polymerization step, is a strong inhibitor of polypeptide synthesis induced by poly U in wheat-germ extracts or by endogenous mRNAs in rat liver cell-free systems. The purified translational inhibitor has shown to be essentially free of proteins. Several chemical and biochemical properties of the inhibition factor have supported the conclusion that it behaves as a 200 bases RNA with a high content of secondary structure. Fil:Fastame, I.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Algranati, I.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_01455680_v44_n3_p475_Fastame
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	protein synthesis inhibitor protozoal RNA animal article genetics isolation and purification Leishmania mexicana metabolism protein synthesis Animals Leishmania mexicana Protein Biosynthesis Protein Synthesis Inhibitors RNA, Protozoan
spellingShingle	protein synthesis inhibitor protozoal RNA animal article genetics isolation and purification Leishmania mexicana metabolism protein synthesis Animals Leishmania mexicana Protein Biosynthesis Protein Synthesis Inhibitors RNA, Protozoan Fastame, I.G. Algranati, I.D. Characterization of a novel translational inhibitor from Leishmania mexicana promastigotes.
topic_facet	protein synthesis inhibitor protozoal RNA animal article genetics isolation and purification Leishmania mexicana metabolism protein synthesis Animals Leishmania mexicana Protein Biosynthesis Protein Synthesis Inhibitors RNA, Protozoan
description	An inhibitory activity blocking protein synthesis elongation in several eukaryotic systems has been detected in Leishmania mexicana extracts. This factor, which competes with aminoacylation of tRNA and also affects the subsequent polymerization step, is a strong inhibitor of polypeptide synthesis induced by poly U in wheat-germ extracts or by endogenous mRNAs in rat liver cell-free systems. The purified translational inhibitor has shown to be essentially free of proteins. Several chemical and biochemical properties of the inhibition factor have supported the conclusion that it behaves as a 200 bases RNA with a high content of secondary structure.
format	JOUR
author	Fastame, I.G. Algranati, I.D.
author_facet	Fastame, I.G. Algranati, I.D.
author_sort	Fastame, I.G.
title	Characterization of a novel translational inhibitor from Leishmania mexicana promastigotes.
title_short	Characterization of a novel translational inhibitor from Leishmania mexicana promastigotes.
title_full	Characterization of a novel translational inhibitor from Leishmania mexicana promastigotes.
title_fullStr	Characterization of a novel translational inhibitor from Leishmania mexicana promastigotes.
title_full_unstemmed	Characterization of a novel translational inhibitor from Leishmania mexicana promastigotes.
title_sort	characterization of a novel translational inhibitor from leishmania mexicana promastigotes.
url	http://hdl.handle.net/20.500.12110/paper_01455680_v44_n3_p475_Fastame
work_keys_str_mv	AT fastameig characterizationofanoveltranslationalinhibitorfromleishmaniamexicanapromastigotes AT algranatiid characterizationofanoveltranslationalinhibitorfromleishmaniamexicanapromastigotes
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Characterization of a novel translational inhibitor from Leishmania mexicana promastigotes.

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