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Characterization of a Novel Association between Two Trypanosome-Specific Proteins and 5S rRNA

P34 and P37 are two previously identified RNA binding proteins in the flagellate protozoan Trypanosoma brucei. RNA interference studies have determined that the proteins are essential and are involved in ribosome biogenesis. Here, we show that these proteins interact in vitro with the 5S rRNA with n...

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Detalles Bibliográficos
Autores principales: Ciganda, Martin, Williams, Noreen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3257258/
https://www.ncbi.nlm.nih.gov/pubmed/22253864
http://dx.doi.org/10.1371/journal.pone.0030029
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author Ciganda, Martin
Williams, Noreen
author_facet Ciganda, Martin
Williams, Noreen
author_sort Ciganda, Martin
collection PubMed
description P34 and P37 are two previously identified RNA binding proteins in the flagellate protozoan Trypanosoma brucei. RNA interference studies have determined that the proteins are essential and are involved in ribosome biogenesis. Here, we show that these proteins interact in vitro with the 5S rRNA with nearly identical binding characteristics in the absence of other cellular factors. The T. brucei 5S rRNA has a complex secondary structure and presents four accessible loops (A to D) for interactions with RNA-binding proteins. In other eukaryotes, loop C is bound by the L5 ribosomal protein and loop A mainly by TFIIIA. The binding of P34 and P37 to T. brucei 5S rRNA involves the LoopA region of the RNA, but these proteins also protect the L5 binding site located on LoopC.
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spelling pubmed-32572582012-01-17 Characterization of a Novel Association between Two Trypanosome-Specific Proteins and 5S rRNA Ciganda, Martin Williams, Noreen PLoS One Research Article P34 and P37 are two previously identified RNA binding proteins in the flagellate protozoan Trypanosoma brucei. RNA interference studies have determined that the proteins are essential and are involved in ribosome biogenesis. Here, we show that these proteins interact in vitro with the 5S rRNA with nearly identical binding characteristics in the absence of other cellular factors. The T. brucei 5S rRNA has a complex secondary structure and presents four accessible loops (A to D) for interactions with RNA-binding proteins. In other eukaryotes, loop C is bound by the L5 ribosomal protein and loop A mainly by TFIIIA. The binding of P34 and P37 to T. brucei 5S rRNA involves the LoopA region of the RNA, but these proteins also protect the L5 binding site located on LoopC. Public Library of Science 2012-01-12 /pmc/articles/PMC3257258/ /pubmed/22253864 http://dx.doi.org/10.1371/journal.pone.0030029 Text en Ciganda, Williams. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Ciganda, Martin
Williams, Noreen
Characterization of a Novel Association between Two Trypanosome-Specific Proteins and 5S rRNA
title Characterization of a Novel Association between Two Trypanosome-Specific Proteins and 5S rRNA
title_full Characterization of a Novel Association between Two Trypanosome-Specific Proteins and 5S rRNA
title_fullStr Characterization of a Novel Association between Two Trypanosome-Specific Proteins and 5S rRNA
title_full_unstemmed Characterization of a Novel Association between Two Trypanosome-Specific Proteins and 5S rRNA
title_short Characterization of a Novel Association between Two Trypanosome-Specific Proteins and 5S rRNA
title_sort characterization of a novel association between two trypanosome-specific proteins and 5s rrna
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3257258/
https://www.ncbi.nlm.nih.gov/pubmed/22253864
http://dx.doi.org/10.1371/journal.pone.0030029
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