TFIP11 Interacts with mDEAH9, an RNA Helicase Involved in Spliceosome Disassembly
| Autor: | Xin Wen, Michael L. Paine, Sissada Tannukit |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
Spliceosome
Nucleolus Protein domain Biology Bioinformatics Article Catalysis lcsh:Chemistry Inorganic Chemistry Dhx15 G-patch Ntr1 Physical and Theoretical Chemistry lcsh:QH301-705.5 Molecular Biology Spectroscopy Spp382 and TFIP11 Organic Chemistry General Medicine RNA Helicase A Yeast Prp43 Computer Science Applications Cell biology spliceosome disassembly mDEAH9 pre-mRNA splicing lcsh:Biology (General) lcsh:QD1-999 RNA splicing Function (biology) Nuclear localization sequence |
| Zdroj: | International Journal of Molecular Sciences; Volume 9; Issue 11; Pages: 2105-2113 International Journal of Molecular Sciences International Journal of Molecular Sciences, Vol 9, Iss 11, Pp 2105-2113 (2008) |
| ISSN: | 1422-0067 |
| DOI: | 10.3390/ijms9112105 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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