MCB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Combs, D. J.
Right arrow Articles by Stevens, S. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Combs, D. J.
Right arrow Articles by Stevens, S. W.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, January 2006, p. 523-534, Vol. 26, No. 2
0270-7306/06/$08.00+0     doi:10.1128/MCB.26.2.523-534.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Prp43p Is a DEAH-Box Spliceosome Disassembly Factor Essential for Ribosome Biogenesis

D. Joshua Combs,1 Roland J. Nagel,2 Manuel Ares Jr.,2 and Scott W. Stevens1,3*

Program in Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas,1 Center for Molecular Biology of RNA, Sinsheimer Laboratories, University of California Santa Cruz, Santa Cruz, California 95064,2 Section in Molecular Genetics and Microbiology and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas3

Received 14 June 2005/ Returned for modification 13 July 2005/ Accepted 17 October 2005

The known function of the DEXH/D-box protein Prp43p is the removal of the U2, U5, and U6 snRNPs from the postsplicing lariat-intron ribonucleoprotein complex. We demonstrate that affinity-purified Prp43p-associated material includes the expected spliceosomal components; however, we also identify several preribosomal complexes that are specifically purified with Prp43p. Conditional prp43 mutant alleles confer a 35S pre-rRNA processing defect, with subsequent depletion of 27S and 20S precursors. Upon a shift to a nonpermissive temperature, both large and small-ribosomal-subunit proteins accumulate in the nucleolus of prp43 mutants. Pulse-chase analysis demonstrates delayed kinetics of 35S, 27S, and 20S pre-rRNA processing with turnover of these intermediates. Microarray analysis of pre-mRNA splicing defects in prp43 mutants shows a very mild effect, similar to that of nonessential pre-mRNA splicing factors. Prp43p is the first DEXH/D-box protein shown to function in both RNA polymerase I and polymerase II transcript metabolism. Its essential function is in its newly characterized role in ribosome biogenesis of both ribosomal subunits, positioning Prp43p to regulate both pre-mRNA splicing and ribosome biogenesis.

* Corresponding author. Mailing address: Institute for Cellular and Molecular Biology, University of Texas at Austin, 1 University Station #A4800, 2500 Speedway 2.448, Austin, TX 78712. Phone: (512) 232-9303. Fax: (512) 232-3432. E-mail: scott.stevens{at}mail.utexas.edu.

Molecular and Cellular Biology, January 2006, p. 523-534, Vol. 26, No. 2
0022-538X/06/$08.00+0     doi:10.1128/MCB.26.2.523-534.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2006 by the American Society for Microbiology. All rights reserved.