Genes and Development

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
QUICK SEARCH:   [advanced]


     

GENES & DEVELOPMENT 19:2991-3003, 2005
©2005 by Cold Spring Harbor Laboratory Press; ISSN 0890-9369/ $5.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Research Data
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Tsai, R.-T.
Right arrow Articles by Cheng, S.-C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tsai, R.-T.
Right arrow Articles by Cheng, S.-C.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

RESEARCH PAPER

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

Rong-Tzong Tsai1,4, Ru-Huei Fu1,4, Fu-Lung Yeh1,4, Chi-Kang Tseng1,3, Yu-Chieh Lin1,2, Yu-hsin Huang1 and Soo-Chen Cheng1,2,3,5

1 Institute of Molecular Biology, and 2 Taiwan International Graduate Program, Molecular and Cellular Biology, Academia Sinica, Nankang, Taipei, Taiwan 115, Republic of China; 3 Institute of Microbiology and Immunology, National Yang-Ming University, Shih-Pai, Taipei, Taiwan 112, Republic of China

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.

[Keywords: Spliceosome disassembly; NTR complex; Prp43; Ntr1; Ntr2]

Received September 21, 2005; revised version accepted October 28, 2005.

Supplemental material is available at http://www.genesdev.org.

Article and publication are at http://www.genesdev.org/cgi/doi/10.1101/gad.1377405.

4 These authors contributed equally to this work.

5 Corresponding author.

E-MAIL mbscc{at}ccvax.sinica.edu.tw; FAX 886-2-27883296.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Mol. Biol. CellHome page
D. Stanek, J. Pridalova-Hnilicova, I. Novotny, M. Huranova, M. Blazikova, X. Wen, A. K. Sapra, and K. M. Neugebauer
Spliceosomal Small Nuclear Ribonucleoprotein Particles Repeatedly Cycle through Cajal Bodies
Mol. Biol. Cell, June 1, 2008; 19(6): 2534 - 2543.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
R.-T. Tsai, C.-K. Tseng, P.-J. Lee, H.-C. Chen, R.-H. Fu, K.-j. Chang, F.-L. Yeh, and S.-C. Cheng
Dynamic Interactions of Ntr1-Ntr2 with Prp43 and with U5 Govern the Recruitment of Prp43 To Mediate Spliceosome Disassembly
Mol. Cell. Biol., December 1, 2007; 27(23): 8027 - 8037.
[Abstract] [Full Text] [PDF]

Home page
 Genes Dev.Home page
N. Tanaka, A. Aronova, and B. Schwer
Ntr1 activates the Prp43 helicase to trigger release of lariat-intron from the spliceosome
Genes & Dev., September 15, 2007; 21(18): 2312 - 2325.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
Y.-C. Liu, H.-C. Chen, N.-Y. Wu, and S.-C. Cheng
A Novel Splicing Factor, Yju2, Is Associated with NTC and Acts after Prp2 in Promoting the First Catalytic Reaction of Pre-mRNA Splicing
Mol. Cell. Biol., August 1, 2007; 27(15): 5403 - 5413.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
G. Herrmann, S. Kais, J. Hoffbauer, K. Shah-Hosseini, N. Bruggenolte, H. Schober, M. Fasi, and P. Schar
Conserved interactions of the splicing factor Ntr1/Spp382 with proteins involved in DNA double-strand break repair and telomere metabolism
Nucleic Acids Res., April 1, 2007; 35(7): 2321 - 2332.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
S. Pandit, B. Lynn, and B. C. Rymond
Inhibition of a spliceosome turnover pathway suppresses splicing defects
PNAS, September 12, 2006; 103(37): 13700 - 13705.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
K.-L. Boon, T. Auchynnikava, G. Edwalds-Gilbert, J. D. Barrass, A. P. Droop, C. Dez, and J. D. Beggs
Yeast ntr1/spp382 mediates prp43 function in postspliceosomes.
Mol. Cell. Biol., August 1, 2006; 26(16): 6016 - 6023.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Genome Res. Learn. Mem.
Protein Science RNA Genes Dev.
Copyright © 2005 by Cold Spring Harbor Laboratory Press.