tfip11 interacts with mdeah9, an rna helicase involved in spliceosome disassemblytfip11与mdeah9,rna解旋酶参与剪接体拆卸.pdfVIP

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tfip11 interacts with mdeah9, an rna helicase involved in spliceosome disassemblytfip11与mdeah9,rna解旋酶参与剪接体拆卸.pdf

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tfip11 interacts with mdeah9, an rna helicase involved in spliceosome disassemblytfip11与mdeah9,rna解旋酶参与剪接体拆卸

Int. J. Mol. Sci. 2008, 9, 2105-2113; DOI: 10.3390/ijms9112105 OPEN ACCESS International Journal of Molecular Sciences ISSN 1422-0067 /journal/ijms/ Article TFIP11 Interacts with mDEAH9, an RNA Helicase Involved in Spliceosome Disassembly Xin Wen, Sissada Tannukit and Michael L. Paine * University of Southern California School of Dentistry, Center for Craniofacial Molecular Biology, 2250 Alcazar Street, CSA room 103, Los Angeles, California 90033-1004, USA. E-Mails: xwen@ (X. W.); tannukit@ (S. T.) * Author to whom correspondence should be addressed; E-mail: paine@; Fax: 1-323-442-2981 Received: 18 August 2008; in revised form: 31 October 2008 / Accepted: 3 November 2008 / Published: 4 November 2008 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 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