Effects of Trypanosoma brucei tryptophanyl-tRNA synthetases silencing by RNA interference

García, Liliana Torcoroma; Leite, Ney Ribeiro; Alfonzo, Juan D.; Thiemann, Otávio Henrique

doi:10.1590/s0074-02762007000600016

Cited by 6 publications

(1 citation statement)

References 2 publications

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“…This construction was linearized by Not I cleavage and transfected into procyclic T. brucei 29-13 (PCF) [19] and T. brucei single marker bloodstream (BSF) [20] cell-lines by electroporation. The cells were cloned by the limiting dilution technique and selected under 2.5 g/mL phleomycin to obtain stable cell lines as previously described [21].…”

Section: Introductionmentioning

confidence: 99%

Oxidative stress protection of Trypanosomes requires selenophosphate synthase

Costa

Oliva

Jesus³

et al. 2011

Molecular and Biochemical Parasitology

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Selenoproteins are characterized by the incorporation of at least one amino acid selenocysteine (Sec-U) encoded by in-frame UGA stop codons. These proteins, as well as the components of the Sec synthesis pathway, are present in members of the bacteria, archaea and eukaryote domains. Although not a ubiquitous pathway in all organisms, it was also identified in several protozoa, including the Kinetoplastida. Genetic evidence has indicated that the pathway is non-essential to the survival of Trypanosoma growing in non-stressed conditions. By analyzing the effects of RNA interference of the Trypanosoma brucei selenophosphate synthetase SPS2, we found a requirement under sub-optimal growth conditions. The present work shows that SPS2 is involved in oxidative stress protection of the parasite and its absence severely hampers the parasite survival in the presence of an oxidizing environment that results in an apoptotic-like phenotype and cell death.

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Section: Introductionmentioning

confidence: 99%

Oxidative stress protection of Trypanosomes requires selenophosphate synthase

Costa

Oliva

Jesus³

et al. 2011

Molecular and Biochemical Parasitology

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Highlights on Trypanosomatid Aminoacyl-tRNA Synthesis

Polycarpo

2013

Subcellular Biochemistry

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Aminoacyl-tRNA synthetases aaRSs are responsible for the aminoacylation of tRNAs in the first step of protein synthesis. They comprise a group of enzymes that catalyze the formation of each possible aminoacyl-tRNA necessary for messenger RNA decoding in a cell. These enzymes have been divided into two classes according to structural features of their active sites and, although each class shares a common active site core, they present an assorted array of appended domains that makes them sufficiently diverse among the different living organisms. Here we will explore what is known about the diversity encountered among trypanosomatids' aaRSs that has helped us not only to understand better the biology of these parasites but can be used rationally for the design of drugs against these protozoa.

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Import of tRNAs and aminoacyl-tRNA synthetases into mitochondria

2008

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During evolution, most of the bacterial genes from the ancestral endosymbiotic alpha-proteobacteria at the origin of mitochondria have been either lost or transferred to the nuclear genome. A crucial evolutionary step was the establishment of macromolecule import systems to allow the come back of proteins and RNAs into the organelle. Paradoxically, the few mitochondria-encoded protein genes remain essential and must be translated by a mitochondrial translation machinery mainly constituted by nucleus-encoded components. Two crucial partners of the mitochondrial translation machinery are the aminoacyl-tRNA synthetases and the tRNAs. All mitochondrial aminoacyl-tRNA synthetases and many tRNAs are imported from the cytosol into the mitochondria in eukaryotic cells. During the last few years, their origin and their import into the organelle have been studied in evolutionary distinct organisms and we review here what is known in this field.

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Effects of Trypanosoma brucei tryptophanyl-tRNA synthetases silencing by RNA interference

Cited by 6 publications

References 2 publications

Oxidative stress protection of Trypanosomes requires selenophosphate synthase

Oxidative stress protection of Trypanosomes requires selenophosphate synthase

Highlights on Trypanosomatid Aminoacyl-tRNA Synthesis

Import of tRNAs and aminoacyl-tRNA synthetases into mitochondria

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