A dataset of proteins associated with Trypanosoma cruzi LYT1 mRNAs
Post-transcriptional gene regulation in Trypanosoma cruzi, the etiological agent of Chagas disease, plays a critical role in ensuring that the parasite successfully completes its life cycle in both of its obligate hosts: insect vector and mammals. This regulation is basically governed by RNA binding...
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| Format: | Article |
| Language: | English |
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Elsevier
2022-04-01
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| Series: | Data in Brief |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2352340922001640 |
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| author | Elizabeth Ruiz Márvez César Augusto Ramírez Segura José María Requena Concepción J. Puerta |
| author_facet | Elizabeth Ruiz Márvez César Augusto Ramírez Segura José María Requena Concepción J. Puerta |
| author_sort | Elizabeth Ruiz Márvez |
| collection | DOAJ |
| description | Post-transcriptional gene regulation in Trypanosoma cruzi, the etiological agent of Chagas disease, plays a critical role in ensuring that the parasite successfully completes its life cycle in both of its obligate hosts: insect vector and mammals. This regulation is basically governed by RNA binding proteins (RBPs) through their interactions with cis-elements located in the UTRs of their mRNA targets. LYT1 gene, coding for a virulence factor of T. cruzi, is expressed into two isoforms: kLYT1 and mLYT1, which play different functions according to their cellular location and parasite life-cycle stages. Whereas kLYT1 exhibits a regulatory role during the epimastigote-to-metacyclic trypomastigote stage transition, mLYT1 acts as a pore-forming protein, relevant for host cell invasion and parasite intracellular survival. Considering the LYT1 biological relevance and the fact that this is a protein exclusive of T. cruzi, the protein and its mechanisms regulating the alternative gene expression products are promising targets for therapeutic intervention. In this work, an experimental approach consisting of pull-downs assays followed by proteomic analyzes was carried out to identify the proteins interacting with the different LYT1 mRNAs. The dataset presented here was obtained through three biological replicates using all the different UTRs characterized in the LYT1 mRNAs (i.e., 5´UTR kLYT1, 5´UTR mLYT1, and I and II-type 3´UTRs) as baits, and protein extracts from epimastigotes and trypomastigotes of the 058 PUJ (DTU I) strain. Bound proteins were analyzed by liquid chromatography coupled to mass spectrometry (LC/MS). As a control of non-specificity, the same protein extracts were incubated with Leishmania braziliensis rRNA and the bound proteins also identified by LC/MS. In all, 1,557 proteins were identified, 313 of them were found in at least two replicates and 18 proteins were exclusively associated with the LYT1 baits. Of these, six proteins have motifs related to RNA binding, and seven remain annotated as hypothetical proteins. Remarkably, three of these hypothetical proteins also contain nucleic acid binding motifs. This knowledge, beside expanding the known T. cruzi proteome, gains insight into putative regulatory proteins responsible for alternative LYT1 mRNAs processing. Raw mass spectrometry data are available via MassIVE proteome Xchange with identifier PXD027371. |
| first_indexed | 2024-12-18T10:47:47Z |
| format | Article |
| id | doaj.art-9b75ed629e29486aaf45768e432a759f |
| institution | Directory Open Access Journal |
| issn | 2352-3409 |
| language | English |
| last_indexed | 2024-12-18T10:47:47Z |
| publishDate | 2022-04-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Data in Brief |
| spelling | doaj.art-9b75ed629e29486aaf45768e432a759f2022-12-21T21:10:32ZengElsevierData in Brief2352-34092022-04-0141107953A dataset of proteins associated with Trypanosoma cruzi LYT1 mRNAsElizabeth Ruiz Márvez0César Augusto Ramírez Segura1José María Requena2Concepción J. Puerta3Departamento de Microbiología, Facultad de Ciencias, Grupo de Investigación en Enfermedades Infecciosas, Pontificia Universidad Javeriana, Carrera 7 # 40- 62, Bogotá, ColombiaDepartamento de Microbiología, Facultad de Ciencias, Grupo de Investigación en Enfermedades Infecciosas, Pontificia Universidad Javeriana, Carrera 7 # 40- 62, Bogotá, ColombiaDepartamento de Biología Molecular, Grupo Regulación de la Expresión Génica en Leishmania del Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Universidad Autónoma de Madrid, Madrid 28049, SpainDepartamento de Microbiología, Facultad de Ciencias, Grupo de Investigación en Enfermedades Infecciosas, Pontificia Universidad Javeriana, Carrera 7 # 40- 62, Bogotá, Colombia; Corresponding author.Post-transcriptional gene regulation in Trypanosoma cruzi, the etiological agent of Chagas disease, plays a critical role in ensuring that the parasite successfully completes its life cycle in both of its obligate hosts: insect vector and mammals. This regulation is basically governed by RNA binding proteins (RBPs) through their interactions with cis-elements located in the UTRs of their mRNA targets. LYT1 gene, coding for a virulence factor of T. cruzi, is expressed into two isoforms: kLYT1 and mLYT1, which play different functions according to their cellular location and parasite life-cycle stages. Whereas kLYT1 exhibits a regulatory role during the epimastigote-to-metacyclic trypomastigote stage transition, mLYT1 acts as a pore-forming protein, relevant for host cell invasion and parasite intracellular survival. Considering the LYT1 biological relevance and the fact that this is a protein exclusive of T. cruzi, the protein and its mechanisms regulating the alternative gene expression products are promising targets for therapeutic intervention. In this work, an experimental approach consisting of pull-downs assays followed by proteomic analyzes was carried out to identify the proteins interacting with the different LYT1 mRNAs. The dataset presented here was obtained through three biological replicates using all the different UTRs characterized in the LYT1 mRNAs (i.e., 5´UTR kLYT1, 5´UTR mLYT1, and I and II-type 3´UTRs) as baits, and protein extracts from epimastigotes and trypomastigotes of the 058 PUJ (DTU I) strain. Bound proteins were analyzed by liquid chromatography coupled to mass spectrometry (LC/MS). As a control of non-specificity, the same protein extracts were incubated with Leishmania braziliensis rRNA and the bound proteins also identified by LC/MS. In all, 1,557 proteins were identified, 313 of them were found in at least two replicates and 18 proteins were exclusively associated with the LYT1 baits. Of these, six proteins have motifs related to RNA binding, and seven remain annotated as hypothetical proteins. Remarkably, three of these hypothetical proteins also contain nucleic acid binding motifs. This knowledge, beside expanding the known T. cruzi proteome, gains insight into putative regulatory proteins responsible for alternative LYT1 mRNAs processing. Raw mass spectrometry data are available via MassIVE proteome Xchange with identifier PXD027371.http://www.sciencedirect.com/science/article/pii/S2352340922001640Alternative trans-splicingInteractomeLYT1 genePull-downRNA-binding proteinsTrypanosoma cruzi |
| spellingShingle | Elizabeth Ruiz Márvez César Augusto Ramírez Segura José María Requena Concepción J. Puerta A dataset of proteins associated with Trypanosoma cruzi LYT1 mRNAs Data in Brief Alternative trans-splicing Interactome LYT1 gene Pull-down RNA-binding proteins Trypanosoma cruzi |
| title | A dataset of proteins associated with Trypanosoma cruzi LYT1 mRNAs |
| title_full | A dataset of proteins associated with Trypanosoma cruzi LYT1 mRNAs |
| title_fullStr | A dataset of proteins associated with Trypanosoma cruzi LYT1 mRNAs |
| title_full_unstemmed | A dataset of proteins associated with Trypanosoma cruzi LYT1 mRNAs |
| title_short | A dataset of proteins associated with Trypanosoma cruzi LYT1 mRNAs |
| title_sort | dataset of proteins associated with trypanosoma cruzi lyt1 mrnas |
| topic | Alternative trans-splicing Interactome LYT1 gene Pull-down RNA-binding proteins Trypanosoma cruzi |
| url | http://www.sciencedirect.com/science/article/pii/S2352340922001640 |
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