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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Proteomic analysis of Trypanosoma cruzi spliceosome complex

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Author(s):
Barbosa, Rosicler L. [1] ; Chagas da Cunha, Julia Pinheiro [2] ; Menezes, Arthur T. [1, 3] ; Melo, Raissa de F. P. [1, 4] ; Elias, Maria Carolina [2] ; Silber, Ariel M. [4] ; Coltri, Patricia P. [1, 3]
Total Authors: 7
Affiliation:
[1] Univ Sao Paulo, Inst Biomed Sci, Dept Cell & Dev Biol, BR-05508000 Sao Paulo - Brazil
[2] Butantan Inst, Ctr Toxins Immune Response & Cell Signalling CeTI, Special Lab Cell Cycle, BR-05503900 Sao Paulo - Brazil
[3] Silber, Ariel M., Univ Sao Paulo, Inst Biomed Sci, Dept Parasitol, Lab Biochem Tryps LaBTryps, BR-05508000 Sao Paulo, Brazil.Barbosa, Rosicler L., Univ Sao Paulo, Inst Biomed Sci, Dept Cell & Dev Biol, BR-05508000 Sao Paulo - Brazil
[4] Univ Sao Paulo, Inst Biomed Sci, Dept Parasitol, Lab Biochem Tryps LaBTryps, BR-05508000 Sao Paulo - Brazil
Total Affiliations: 4
Document type: Journal article
Source: JOURNAL OF PROTEOMICS; v. 223, JUL 15 2020.
Web of Science Citations: 0
Abstract

The unicellular protists of the group Kinetoplastida include the genera Leishmania and Trypanosoma, which are pathogens of invertebrate and vertebrate animals. Despite their medical and economical importance, critical aspects of their biology such as specific molecular characteristics of gene expression regulation are just beginning to be deciphered. Gene expression regulation also depends on post-transcriptional processing steps, such as the trans-splicing process. Despite being widely used in trypanosomes, trans-splicing is a rare event in other eukaryotes. We sought to describe the protein composition of spliceosomes in epimastigotes of T. cruzi, the etiological agent of Chagas disease. We used two TAP-tagged proteins to affinity purify spliceosomes and analyzed their composition by mass spectrometry. Among the 115 identified proteins we detected conserved spliceosome components, as Sm and LSm proteins, RNA helicases, U2- and U5-snRNP specific proteins. Importantly, by comparing our data with proteomic data of human and T. brucei spliceosome complexes, we observed a core group of proteins common to all spliceosomes. By using amino acid sequence comparisons, we identified RNA-associated proteins that might be involved with splicing regulation in T. cruzi, namely the orthologous of WDR33, PABPCL1 and three different HNRNPs. Data are available via ProteomeXchange with identifier PXD018776. (AU)

FAPESP's process: 17/06994-9 - MicroRNA splicing regulation in eukaryotes
Grantee:Patricia Pereira Coltri
Support Opportunities: Regular Research Grants
FAPESP's process: 17/16553-0 - The role of the mitochondrial and glycosomal isoforms of fumarate reductase of Trypanosoma Cruzi
Grantee:Ariel Mariano Silber
Support Opportunities: Research Grants - Visiting Researcher Grant - International
FAPESP's process: 16/06034-2 - The biological role of amino acids and their metabolites in Trypanosoma cruzi
Grantee:Ariel Mariano Silber
Support Opportunities: Research Projects - Thematic Grants