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Int. J. Mol. Sci. 2008, 9(11), 2105-2113; doi:10.3390/ijms9112105

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

University of Southern California School of Dentistry, Center for Craniofacial Molecular Biology, 2250 Alcazar Street, CSA room 103, Los Angeles, California 90033-1004, USA
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Received: 18 August 2008 / Revised: 31 October 2008 / Accepted: 3 November 2008 / Published: 4 November 2008
(This article belongs to the Section Biochemistry, Molecular Biology and Biophysics)
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Abstract

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 latestage 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. View Full-Text
Keywords: mDEAH9; Dhx15; G-patch; Ntr1; pre-mRNA splicing; Prp43; spliceosome disassembly; Spp382 and TFIP11 mDEAH9; Dhx15; G-patch; Ntr1; pre-mRNA splicing; Prp43; spliceosome disassembly; Spp382 and TFIP11
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This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Wen, X.; Tannukit, S.; Paine, M.L. TFIP11 Interacts with mDEAH9, an RNA Helicase Involved in Spliceosome Disassembly. Int. J. Mol. Sci. 2008, 9, 2105-2113.

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