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TFIP11 Interacts with mDEAH9, an RNA Helicase Involved in Spliceosome Disassembly

Yeast proteins Ntr1, Ntr2 and Prp43 function in spliceosome disassembly. An Ntr1-Ntr2 protein complex recruits Prp43 to allow the removal of the lariat-intron in late-stage RNA splicing activity. Based on amino-acid sequence similarities across species, TFIP11 and mDEAH9/Dhx15 have been identified a...

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Detalles Bibliográficos
Autores principales: Wen, Xin, Tannukit, Sissada, Paine, Michael L.
Formato: Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2629433/
https://www.ncbi.nlm.nih.gov/pubmed/19165350
http://dx.doi.org/10.3390/ijms9112105
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author Wen, Xin
Tannukit, Sissada
Paine, Michael L.
author_facet Wen, Xin
Tannukit, Sissada
Paine, Michael L.
author_sort Wen, Xin
collection PubMed
description Yeast proteins Ntr1, Ntr2 and Prp43 function in spliceosome disassembly. An Ntr1-Ntr2 protein complex recruits Prp43 to allow the removal of the lariat-intron in late-stage RNA splicing activity. Based on amino-acid sequence similarities across species, TFIP11 and mDEAH9/Dhx15 have been identified as homologues of yeast Ntr1 and Prp43, respectively. The N-terminal region of TFIP11 contains a G-patch, which is a highly conserved domain of many RNA-processing proteins. TFIP11 displays a unique and characteristic subnuclear localization pattern, in close proximity to SC35 nuclear speckles. Transfected GFP-tagged mDEAH9 displays an evenly distributed nuclear localization and is excluded from the nucleoli; however when TFIP11 and mDEAH9 are co-transfected, both proteins colocalize to distinct nuclear speckles. These data show that TFIP11 recruits mDEAH9 suggesting that these two proteins have similar biological activities to their yeast counterparts.
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spelling pubmed-26294332009-03-25 TFIP11 Interacts with mDEAH9, an RNA Helicase Involved in Spliceosome Disassembly Wen, Xin Tannukit, Sissada Paine, Michael L. Int J Mol Sci Article Yeast proteins Ntr1, Ntr2 and Prp43 function in spliceosome disassembly. An Ntr1-Ntr2 protein complex recruits Prp43 to allow the removal of the lariat-intron in late-stage RNA splicing activity. Based on amino-acid sequence similarities across species, TFIP11 and mDEAH9/Dhx15 have been identified as homologues of yeast Ntr1 and Prp43, respectively. The N-terminal region of TFIP11 contains a G-patch, which is a highly conserved domain of many RNA-processing proteins. TFIP11 displays a unique and characteristic subnuclear localization pattern, in close proximity to SC35 nuclear speckles. Transfected GFP-tagged mDEAH9 displays an evenly distributed nuclear localization and is excluded from the nucleoli; however when TFIP11 and mDEAH9 are co-transfected, both proteins colocalize to distinct nuclear speckles. These data show that TFIP11 recruits mDEAH9 suggesting that these two proteins have similar biological activities to their yeast counterparts. Molecular Diversity Preservation International (MDPI) 2008-11-04 /pmc/articles/PMC2629433/ /pubmed/19165350 http://dx.doi.org/10.3390/ijms9112105 Text en © 2008 by MDPI http://creativecommons.org/licenses/by/3.0 This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Wen, Xin
Tannukit, Sissada
Paine, Michael L.
TFIP11 Interacts with mDEAH9, an RNA Helicase Involved in Spliceosome Disassembly
title TFIP11 Interacts with mDEAH9, an RNA Helicase Involved in Spliceosome Disassembly
title_full TFIP11 Interacts with mDEAH9, an RNA Helicase Involved in Spliceosome Disassembly
title_fullStr TFIP11 Interacts with mDEAH9, an RNA Helicase Involved in Spliceosome Disassembly
title_full_unstemmed TFIP11 Interacts with mDEAH9, an RNA Helicase Involved in Spliceosome Disassembly
title_short TFIP11 Interacts with mDEAH9, an RNA Helicase Involved in Spliceosome Disassembly
title_sort tfip11 interacts with mdeah9, an rna helicase involved in spliceosome disassembly
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2629433/
https://www.ncbi.nlm.nih.gov/pubmed/19165350
http://dx.doi.org/10.3390/ijms9112105
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