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Molecular and Cellular Biology, December 2007, p. 8027-8037, Vol. 27, No. 23
0270-7306/07/$08.00+0     doi:10.1128/MCB.01213-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Dynamic Interactions of Ntr1-Ntr2 with Prp43 and with U5 Govern the Recruitment of Prp43 To Mediate Spliceosome Disassembly{triangledown}

Rong-Tzong Tsai,1,{dagger},{ddagger} Chi-Kang Tseng,1,2,{ddagger} Pei-Jung Lee,1 Hsin-Chou Chen,1 Ru-Huei Fu,1 Kae-jiun Chang,1 Fu-Lung Yeh,1 and Soo-Chen Cheng1,2*

Institute of Molecular Biology, Academia Sinica, Nankang, Taipei, Taiwan, Republic of China,1 Institute of Microbiology and Immunology, National Yang-Ming University, Shih-Pai, Taipei, Taiwan, Republic of China2

Received 9 July 2007/ Returned for modification 10 August 2007/ Accepted 12 September 2007

The Saccharomyces cerevisiae splicing factors Ntr1 (also known as Spp382) and Ntr2 form a stable complex and can further associate with DExD/H-box RNA helicase Prp43 to form a functional complex, termed the NTR complex, which catalyzes spliceosome disassembly. We show that Prp43 interacts with Ntr1-Ntr2 in a dynamic manner. The Ntr1-Ntr2 complex can also bind to the spliceosome first, before recruiting Prp43 to catalyze disassembly. Binding of Ntr1-Ntr2 or Prp43 does not require ATP, but disassembly of the spliceosome requires hydrolysis of ATP. The NTR complex also dynamically interacts with U5 snRNP. Ntr2 interacts with U5 component Brr2 and is essential for both interactions of NTR with U5 and with the spliceosome. Ntr2 alone can also bind to U5 and to the spliceosome, suggesting a role of Ntr2 in mediating the binding of NTR to the spliceosome through its interaction with U5. Our results demonstrate that dynamic interactions of NTR with U5, through the interaction of Ntr2 with Brr2, and interactions of Ntr1 and Prp43 govern the recruitment of Prp43 to the spliceosome to mediate spliceosome disassembly.

* Corresponding author. Mailing address: Institute of Molecular Biology, Academia Sinica, Nankang, Taipei, Taiwan, Republic of China. Phone: 886-2-2789-9200. Fax: 886-2-2788-3296. E-mail: mbscc{at}ccvax.sinica.edu.tw

{triangledown} Published ahead of print on 24 September 2007.

{dagger} Present address: Institute of Biochemistry and Biotechnology, Chung Shan Medical University, Taichung, Taiwan, Republic of China.

{ddagger} These authors contributed equally to this study.

Molecular and Cellular Biology, December 2007, p. 8027-8037, Vol. 27, No. 23
0270-7306/07/$08.00+0     doi:10.1128/MCB.01213-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Yoshimoto, R., Kataoka, N., Okawa, K., Ohno, M. (2009). Isolation and characterization of post-splicing lariat-intron complexes. Nucleic Acids Res 37: 891-902 [Abstract] [Full Text]  
  • Stanek, D., Pridalova-Hnilicova, J., Novotny, I., Huranova, M., Blazikova, M., Wen, X., Sapra, A. K., Neugebauer, K. M. (2008). Spliceosomal Small Nuclear Ribonucleoprotein Particles Repeatedly Cycle through Cajal Bodies. Mol. Biol. Cell 19: 2534-2543 [Abstract] [Full Text]  


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