Identification of novel proteins and mRNAs differentially bound to the Leishmania Poly(A) Binding Proteins reveals a direct association between PABP1, the RNA-binding protein RBP23 and mRNAs encoding ribosomal proteins

dc.creatorAssis, Ludmila A.
dc.creatorSantos Filho, Moezio V. C.
dc.creatorSilva, Joao R. da Cruz
dc.creatorBezerra, Maria J. R.
dc.creatorAquino, Irassandra R. P. U. C. de
dc.creatorMerlo, Kleison C.
dc.creatorHoletz, Fabíola Barbieri
dc.creatorProbst, Christian Macagnan
dc.creatorRezende, Antonio M.
dc.creatorPapadopoulou, Barbara
dc.creatorLima, Tamara D. C. da Costa
dc.creatorMelo Neto, Osvaldo P. de
dc.date2021-12-13T19:47:17Z
dc.date2021-12-13T19:47:17Z
dc.date2021
dc.date.accessioned2023-09-26T20:08:20Z
dc.date.available2023-09-26T20:08:20Z
dc.identifierASSIS, Ludmila A. et al. Identification of novel proteins and mRNAs differentially bound to the Leishmania Poly(A) binding proteins reveals a direct association between PABP1, the RNA-binding protein RBP23 and mRNAs encoding ribosomal proteins. PLOS Neglected Tropical Diseases, v.15, n.10, p. 1–30, 2021.
dc.identifier1935-2735
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/50377
dc.identifier10.1371/journal.pntd.0009899
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8849465
dc.descriptionPoly(A) Binding Proteins (PABPs) are major eukaryotic RNA-binding proteins (RBPs) with multiple roles associated with mRNA stability and translation and characterized mainly from multicellular organisms and yeasts. A variable number of PABP homologues are seen in different organisms however the biological reasons for multiple PABPs are generally not well understood. In the unicellular Leishmania, dependent on post-transcriptional mechanisms for the control of its gene expression, three distinct PABPs are found, with yet undefined functional distinctions. Here, using RNA-immunoprecipitation sequencing analysis we show that the Leishmania PABP1 preferentially associates with mRNAs encoding ribosomal proteins, while PABP2 and PABP3 bind to an overlapping set of mRNAs distinct to those enriched in PABP1. Immunoprecipitation studies combined to mass-spectrometry analysis identified RBPs differentially associated with PABP1 or PABP2, including RBP23 and DRBD2, respectively, that were investigated further. Both RBP23 and DRBD2 bind directly to the three PABPs in vitro, but reciprocal experiments confirmed preferential co-immunoprecipitation of PABP1, as well as the EIF4E4/EIF4G3 based translation initiation complex, with RBP23. Other RBP23 binding partners also imply a direct role in translation. DRBD2, in contrast, co-immunoprecipitated with PABP2, PABP3 and with RBPs unrelated to translation. Over 90% of the RBP23-bound mRNAs code for ribosomal proteins, mainly absent from the transcripts co-precipitated with DRBD2. These experiments suggest a novel and specific route for translation of the ribosomal protein mRNAs, mediated by RBP23, PABP1.
dc.formatapplication/pdf
dc.languagepor
dc.publisherPublic Library of Science
dc.rightsopen access
dc.subjectPoly(A)-Binding Protein I
dc.subjectProtein Biosynthesis
dc.subjectTranslation, mRNA
dc.subjectRibosomal Proteins
dc.subjectProteína I de Unión a Poli(A)
dc.subjectBiosíntesis de Proteínas
dc.subjectProteínas Ribosómicas
dc.subjectProtéine-1 de liaison au poly(A)
dc.subjectBiosynthèse des protéines
dc.subjectProtéines ribosomiques
dc.subjectProteína I de Ligação a Poli(A)
dc.subjectBiossíntese de Proteínas
dc.subjectProteínas Ribossômicas
dc.subjectLeishmania
dc.titleIdentification of novel proteins and mRNAs differentially bound to the Leishmania Poly(A) Binding Proteins reveals a direct association between PABP1, the RNA-binding protein RBP23 and mRNAs encoding ribosomal proteins
dc.typeArticle


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