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 Granneman, S.
Right arrow Articles by Baserga, S. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Granneman, S.
Right arrow Articles by Baserga, S. J.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, February 2006, p. 1183-1194, Vol. 26, No. 4
0270-7306/06/$08.00+0     doi:10.1128/MCB.26.4.1183-1194.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Comprehensive Mutational Analysis of Yeast DEXD/H Box RNA Helicases Required for Small Ribosomal Subunit Synthesis

Sander Granneman,1 Kara A. Bernstein,2 Franziska Bleichert,2 and Susan J. Baserga1,2,3*

Departments of Molecular Biophysics and Biochemistry,1 Genetics,2 Therapeutic Radiology, Yale University School of Medicine, New Haven, Connecticut 065203

Received 25 July 2005/ Returned for modification 19 August 2005/ Accepted 14 November 2005

The 17 putative RNA helicases required for pre-rRNA processing are predicted to play a crucial role in ribosome biogenesis by driving structural rearrangements within preribosomes. To better understand the function of these proteins, we have generated a battery of mutations in five putative RNA helicases involved in 18S rRNA synthesis and analyzed their effects on cell growth and pre-rRNA processing. Our results define functionally important residues within conserved motifs and demonstrate that lethal mutations in predicted ATP binding-hydrolysis motifs often confer a dominant negative phenotype in vivo when overexpressed in a wild-type background. We show that dominant negative mutants delay processing of the 35S pre-rRNA and cause accumulation of pre-rRNA species that normally have low steady-state levels. Our combined results establish that not all conserved domains function identically in each protein, suggesting that the RNA helicases may have distinct biochemical properties and diverse roles in ribosome biogenesis.


* Corresponding author. Mailing address: Molecular Biophysics & Biochemistry Department, Yale University School of Medicine, 333 Cedar St., SHM C-114, New Haven, CT 06520-8024. Phone: (203) 785-4618. Fax: (203) 785-6404. E-mail: susan.baserga{at}yale.edu.


Molecular and Cellular Biology, February 2006, p. 1183-1194, Vol. 26, No. 4
0022-538X/06/$08.00+0     doi:10.1128/MCB.26.4.1183-1194.2006
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.