Identification of a novel nucleocytoplasmic shuttling RNA helicase of trypanosomes.

Gene expression in trypanosomes is controlled mostly by post-transcriptional pathways. Little is known about the components of mRNA nucleocytoplasmic export routes in these parasites. Comparative genomics has shown that the mRNA transport pathway is the least conserved pathway among eukaryotes. None...

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Autores principales: Alexandre Haruo Inoue, Mariana Serpeloni, Priscila Mazzocchi Hiraiwa, Sueli Fumie Yamada-Ogatta, João Renato Carvalho Muniz, Maria Cristina Machado Motta, Newton Medeiros Vidal, Samuel Goldenberg, Andréa Rodrigues Avila
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Publicado: Public Library of Science (PLoS) 2014
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spelling oai:doaj.org-article:3290843a5e7d4730a987c7017225391f2021-11-25T05:56:46ZIdentification of a novel nucleocytoplasmic shuttling RNA helicase of trypanosomes.1932-620310.1371/journal.pone.0109521https://doaj.org/article/3290843a5e7d4730a987c7017225391f2014-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0109521https://doaj.org/toc/1932-6203Gene expression in trypanosomes is controlled mostly by post-transcriptional pathways. Little is known about the components of mRNA nucleocytoplasmic export routes in these parasites. Comparative genomics has shown that the mRNA transport pathway is the least conserved pathway among eukaryotes. Nonetheless, we identified a RNA helicase (Hel45) that is conserved across eukaryotes and similar to shuttling proteins involved in mRNA export. We used in silico analysis to predict the structure of Trypanosoma cruzi Hel45, including the N-terminal domain and the C-terminal domain, and our findings suggest that this RNA helicase can form complexes with mRNA. Hel45 was present in both nucleus and cytoplasm. Electron microscopy showed that Hel45 is clustered close to the cytoplasmic side of nuclear pore complexes, and is also present in the nucleus where it is associated with peripheral compact chromatin. Deletion of a predicted Nuclear Export Signal motif led to the accumulation of Hel45ΔNES in the nucleus, indicating that Hel45 shuttles between the nucleus and the cytoplasm. This transport was dependent on active transcription but did not depend on the exportin Crm1. Knockdown of Mex67 in T. brucei caused the nuclear accumulation of the T. brucei ortholog of Hel45. Indeed, Hel45 is present in mRNA ribonucleoprotein complexes that are not associated with polysomes. It is still necessary to confirm the precise function of Hel45. However, this RNA helicase is associated with mRNA metabolism and its nucleocytoplasmic shuttling is dependent on an mRNA export route involving Mex67 receptor.Alexandre Haruo InoueMariana SerpeloniPriscila Mazzocchi HiraiwaSueli Fumie Yamada-OgattaJoão Renato Carvalho MunizMaria Cristina Machado MottaNewton Medeiros VidalSamuel GoldenbergAndréa Rodrigues AvilaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 10, p e109521 (2014)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Alexandre Haruo Inoue
Mariana Serpeloni
Priscila Mazzocchi Hiraiwa
Sueli Fumie Yamada-Ogatta
João Renato Carvalho Muniz
Maria Cristina Machado Motta
Newton Medeiros Vidal
Samuel Goldenberg
Andréa Rodrigues Avila
Identification of a novel nucleocytoplasmic shuttling RNA helicase of trypanosomes.
description Gene expression in trypanosomes is controlled mostly by post-transcriptional pathways. Little is known about the components of mRNA nucleocytoplasmic export routes in these parasites. Comparative genomics has shown that the mRNA transport pathway is the least conserved pathway among eukaryotes. Nonetheless, we identified a RNA helicase (Hel45) that is conserved across eukaryotes and similar to shuttling proteins involved in mRNA export. We used in silico analysis to predict the structure of Trypanosoma cruzi Hel45, including the N-terminal domain and the C-terminal domain, and our findings suggest that this RNA helicase can form complexes with mRNA. Hel45 was present in both nucleus and cytoplasm. Electron microscopy showed that Hel45 is clustered close to the cytoplasmic side of nuclear pore complexes, and is also present in the nucleus where it is associated with peripheral compact chromatin. Deletion of a predicted Nuclear Export Signal motif led to the accumulation of Hel45ΔNES in the nucleus, indicating that Hel45 shuttles between the nucleus and the cytoplasm. This transport was dependent on active transcription but did not depend on the exportin Crm1. Knockdown of Mex67 in T. brucei caused the nuclear accumulation of the T. brucei ortholog of Hel45. Indeed, Hel45 is present in mRNA ribonucleoprotein complexes that are not associated with polysomes. It is still necessary to confirm the precise function of Hel45. However, this RNA helicase is associated with mRNA metabolism and its nucleocytoplasmic shuttling is dependent on an mRNA export route involving Mex67 receptor.
format article
author Alexandre Haruo Inoue
Mariana Serpeloni
Priscila Mazzocchi Hiraiwa
Sueli Fumie Yamada-Ogatta
João Renato Carvalho Muniz
Maria Cristina Machado Motta
Newton Medeiros Vidal
Samuel Goldenberg
Andréa Rodrigues Avila
author_facet Alexandre Haruo Inoue
Mariana Serpeloni
Priscila Mazzocchi Hiraiwa
Sueli Fumie Yamada-Ogatta
João Renato Carvalho Muniz
Maria Cristina Machado Motta
Newton Medeiros Vidal
Samuel Goldenberg
Andréa Rodrigues Avila
author_sort Alexandre Haruo Inoue
title Identification of a novel nucleocytoplasmic shuttling RNA helicase of trypanosomes.
title_short Identification of a novel nucleocytoplasmic shuttling RNA helicase of trypanosomes.
title_full Identification of a novel nucleocytoplasmic shuttling RNA helicase of trypanosomes.
title_fullStr Identification of a novel nucleocytoplasmic shuttling RNA helicase of trypanosomes.
title_full_unstemmed Identification of a novel nucleocytoplasmic shuttling RNA helicase of trypanosomes.
title_sort identification of a novel nucleocytoplasmic shuttling rna helicase of trypanosomes.
publisher Public Library of Science (PLoS)
publishDate 2014
url https://doaj.org/article/3290843a5e7d4730a987c7017225391f
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