Spliceosome disassembly catalyzed by Prp43 and its associated components Ntr1 and Ntr2

doi:10.1101/gad.1377405

中山醫學大學機構典藏 CSMUIR > 醫學院 > 生化微生物免疫研究所 > 期刊論文 > Item 310902500/11624

Please use this identifier to cite or link to this item: https://ir.csmu.edu.tw:8080/ir/handle/310902500/11624

Title:	Spliceosome disassembly catalyzed by Prp43 and its associated components Ntr1 and Ntr2
Authors:	Tsai, Rong-Tzong Fu1, Ru-Huei Yeh1, Fu-Lung Tseng1, Chi-Kang Lin1, Yu-Chieh Huang, Yu-hsin Cheng, Soo-Chen
Contributors:	中山醫學大學
Keywords:	Spliceosome disassembly NTR complex Prp43 Ntr1 Ntr2
Date:	2005
Issue Date:	2015-07-24T09:10:24Z (UTC)
ISSN:	0890-9369
Abstract:	Two novel yeast splicing factors required for spliceosome disassembly have been identified. Ntr1 and Ntr2 (NineTeen complex-Related proteins) were identified for their weak association with components of the Prp19-associated complex. Unlike other Prp19-associated components, these two proteins were primarily associated with the intron-containing spliceosome during the splicing reaction. Extracts depleted of Ntr1 or Ntr2 exhibited full splicing activity, but accumulated large amounts of lariat-intron in the spliceosome after splicing, indicating that the normal function of the Prp19-associated complex in spliceosome activation was not affected, but spliceosome disassembly was hindered. Immunoprecipitation analysis revealed that Ntr1 and Ntr2 formed a stable complex with DExD/H-box RNA helicase Prp43 in the splicing extract. Ntr1 interacted with Prp43 through the N-terminal G-patch domain, with Ntr2 through a middle region, and with itself through the carboxyl half of the protein. The affinity-purified Ntr1–Ntr2–Prp43 complex could catalyze disassembly of the spliceosome in an ATP-dependent manner, separating U2, U5, U6, NTC (NineTeen Complex), and lariat-intron. This is the first demonstration of physical disassembly of the spliceosome, catalyzed by a complex containing a DExD/H-box RNA helicase and two accessory factors, which might function in targeting the helicase to the correct substrate.
URI:	https://ir.csmu.edu.tw:8080/ir/handle/310902500/11624 http://dx.doi.org/10.1101/gad.1377405
Relation:	Genes & Dev. 2005. 19: 2991-3003
Appears in Collections:	[生化微生物免疫研究所] 期刊論文

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