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Trypanosome MTR4 is involved in rRNA processing

The yeast putative RNA helicase Mtr4p is implicated in exosome-mediated RNA quality control in the nucleus, interacts with the exosome, and is found in the ‘TRAMP’ complex with a yeast nuclear poly(A) polymerase (Trf4p/Pap2p or Trf5p) and a putative RNA-binding protein, Air1p or Air2p. Depletion of...

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Detalles Bibliográficos
Autores principales: Cristodero, Marina, Clayton, Christine E.
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2007
Materias:
RNA
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2175323/
https://www.ncbi.nlm.nih.gov/pubmed/17940093
http://dx.doi.org/10.1093/nar/gkm736
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author Cristodero, Marina
Clayton, Christine E.
author_facet Cristodero, Marina
Clayton, Christine E.
author_sort Cristodero, Marina
collection PubMed
description The yeast putative RNA helicase Mtr4p is implicated in exosome-mediated RNA quality control in the nucleus, interacts with the exosome, and is found in the ‘TRAMP’ complex with a yeast nuclear poly(A) polymerase (Trf4p/Pap2p or Trf5p) and a putative RNA-binding protein, Air1p or Air2p. Depletion of the Trypanosoma brucei MTR4-like protein TbMTR4 caused growth arrest and defects in 5.8S rRNA processing similar to those seen after depletion of the exosome. TbNPAPL, a nuclear protein which is a putative homolog of Trf4p/Pap2p, was required for normal cell growth. Depletion of MTR4 resulted in the accumulation of polyadenylated rRNA precursors, while depletion of TbNPAPL had little effect. These results suggest that polyadenylation-dependent nuclear rRNA quality control is conserved in eukaryotic evolution. In contrast, there was no evidence for a trypanosome TRAMP complex since no stable interactions between TbMTR4 and the exosome, TbNPAPL or RNA-binding proteins were detected.
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spelling pubmed-21753232008-01-07 Trypanosome MTR4 is involved in rRNA processing Cristodero, Marina Clayton, Christine E. Nucleic Acids Res RNA The yeast putative RNA helicase Mtr4p is implicated in exosome-mediated RNA quality control in the nucleus, interacts with the exosome, and is found in the ‘TRAMP’ complex with a yeast nuclear poly(A) polymerase (Trf4p/Pap2p or Trf5p) and a putative RNA-binding protein, Air1p or Air2p. Depletion of the Trypanosoma brucei MTR4-like protein TbMTR4 caused growth arrest and defects in 5.8S rRNA processing similar to those seen after depletion of the exosome. TbNPAPL, a nuclear protein which is a putative homolog of Trf4p/Pap2p, was required for normal cell growth. Depletion of MTR4 resulted in the accumulation of polyadenylated rRNA precursors, while depletion of TbNPAPL had little effect. These results suggest that polyadenylation-dependent nuclear rRNA quality control is conserved in eukaryotic evolution. In contrast, there was no evidence for a trypanosome TRAMP complex since no stable interactions between TbMTR4 and the exosome, TbNPAPL or RNA-binding proteins were detected. Oxford University Press 2007-11 2007-10-16 /pmc/articles/PMC2175323/ /pubmed/17940093 http://dx.doi.org/10.1093/nar/gkm736 Text en © 2007 The Author(s) http://creativecommons.org/licenses/by-nc/2.0/uk/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle RNA
Cristodero, Marina
Clayton, Christine E.
Trypanosome MTR4 is involved in rRNA processing
title Trypanosome MTR4 is involved in rRNA processing
title_full Trypanosome MTR4 is involved in rRNA processing
title_fullStr Trypanosome MTR4 is involved in rRNA processing
title_full_unstemmed Trypanosome MTR4 is involved in rRNA processing
title_short Trypanosome MTR4 is involved in rRNA processing
title_sort trypanosome mtr4 is involved in rrna processing
topic RNA
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2175323/
https://www.ncbi.nlm.nih.gov/pubmed/17940093
http://dx.doi.org/10.1093/nar/gkm736
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