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 Fewell, S. W.
Right arrow Articles by Woolford, J. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fewell, S. W.
Right arrow Articles by Woolford, J. L., Jr.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, January 1999, p. 826-834, Vol. 19, No. 1
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Ribosomal Protein S14 of Saccharomyces cerevisiae Regulates Its Expression by Binding to RPS14B Pre-mRNA and to 18S rRNA

Sheara W. Fewell and John L. Woolford Jr.*

Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213

Received 29 July 1998/Returned for modification 26 August 1998/Accepted 24 September 1998

Production of ribosomal protein S14 in Saccharomyces cerevisiae is coordinated with the rate of ribosome assembly by a feedback mechanism that represses expression of RPS14B. Three-hybrid assays in vivo and filter binding assays in vitro demonstrate that rpS14 directly binds to an RNA stem-loop structure in RPS14B pre-mRNA that is necessary for RPS14B regulation. Moreover, rpS14 binds to a conserved helix in 18S rRNA with approximately five- to sixfold-greater affinity. These results support the model that RPS14B regulation is mediated by direct binding of rpS14 either to its pre-mRNA or to rRNA. Investigation of these interactions with the three-hybrid system reveals two regions of rpS14 that are involved in RNA recognition. D52G and E55G mutations in rpS14 alter the specificity of rpS14 for RNA, as indicated by increased affinity for RPS14B RNA but reduced affinity for the rRNA target. Deletion of the C terminus of rpS14, where multiple antibiotic resistance mutations map, prevents binding of rpS14 to RNA and production of functional 40S subunits. The emetine-resistant protein, rpS14-EmRR, which contains two mutations near the C terminus of rpS14, does not bind either RNA target in the three-hybrid or in vitro assays. This is the first direct demonstration that an antibiotic resistance mutation alters binding of an r protein to rRNA and is consistent with the hypothesis that antibiotic resistance mutations can result from local alterations in rRNA structure.


* Corresponding author. Mailing address: Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15213. Phone: (412) 268-3193. Fax: (412) 268-7129. E-mail: JW17{at}andrew.cmu.edu.


Molecular and Cellular Biology, January 1999, p. 826-834, Vol. 19, No. 1
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Malygin, A. A., Parakhnevitch, N. M., Ivanov, A. V., Eperon, I. C., Karpova, G. G. (2007). Human ribosomal protein S13 regulates expression of its own gene at the splicing step by a feedback mechanism. Nucleic Acids Res 35: 6414-6423 [Abstract] [Full Text]  
  • Phatnani, H. P., Greenleaf, A. L. (2006). Phosphorylation and functions of the RNA polymerase II CTD.. Genes Dev. 20: 2922-2936 [Abstract] [Full Text]  
  • Bassler, J., Kallas, M., Hurt, E. (2006). The NUG1 GTPase Reveals an N-terminal RNA-binding Domain That Is Essential for Association with 60 S Pre-ribosomal Particles. J. Biol. Chem. 281: 24737-24744 [Abstract] [Full Text]  
  • Ni, J.-Q., Liu, L.-P., Hess, D., Rietdorf, J., Sun, F.-L. (2006). Drosophila ribosomal proteins are associated with linker histone H1 and suppress gene transcription. Genes Dev. 20: 1959-1973 [Abstract] [Full Text]  
  • Preker, P. J., Guthrie, C. (2006). Autoregulation of the mRNA export factor Yra1p requires inefficient splicing of its pre-mRNA. RNA 12: 994-1006 [Abstract] [Full Text]  
  • Cuccurese, M., Russo, G., Russo, A., Pietropaolo, C. (2005). Alternative splicing and nonsense-mediated mRNA decay regulate mammalian ribosomal gene expression. Nucleic Acids Res 33: 5965-5977 [Abstract] [Full Text]  
  • SCHRODER, P. A., MOORE, M. J. (2005). Association of ribosomal proteins with nascent transcripts in S. cerevisiae. RNA 11: 1521-1529 [Abstract] [Full Text]  
  • Webb, C. J., Lakhe-Reddy, S., Romfo, C. M., Wise, J. A. (2005). Analysis of Mutant Phenotypes and Splicing Defects Demonstrates Functional Collaboration between the Large and Small Subunits of the Essential Splicing Factor U2AF In Vivo. Mol. Biol. Cell 16: 584-596 [Abstract] [Full Text]  
  • Webb, C. J., Romfo, C. M., van Heeckeren, W. J., Wise, J. A. (2005). Exonic splicing enhancers in fission yeast: functional conservation demonstrates an early evolutionary origin. Genes Dev. 19: 242-254 [Abstract] [Full Text]  
  • Bernstein, K. A., Baserga, S. J. (2004). The Small Subunit Processome Is Required for Cell Cycle Progression at G1. Mol. Biol. Cell 15: 5038-5046 [Abstract] [Full Text]  
  • Casati, P., Walbot, V. (2004). Crosslinking of Ribosomal Proteins to RNA in Maize Ribosomes by UV-B and Its Effects on Translation. Plant Physiol. 136: 3319-3332 [Abstract] [Full Text]  
  • Webb, C. J., Wise, J. A. (2004). The Splicing Factor U2AF Small Subunit Is Functionally Conserved between Fission Yeast and Humans. Mol. Cell. Biol. 24: 4229-4240 [Abstract] [Full Text]  
  • Mauro, V. P., Edelman, G. M. (2002). The ribosome filter hypothesis. Proc. Natl. Acad. Sci. USA 99: 12031-12036 [Abstract] [Full Text]  
  • Carr-Schmid, A., Pfund, C., Craig, E. A., Kinzy, T. G. (2002). Novel G-Protein Complex Whose Requirement Is Linked to the Translational Status of the Cell. Mol. Cell. Biol. 22: 2564-2574 [Abstract] [Full Text]  
  • Hendrick, J. L., Wilson, P. G., Edelman, I. I., Sandbaken, M. G., Ursic, D., Culbertson, M. R. (2001). Yeast Frameshift Suppressor Mutations in the Genes Coding for Transcription Factor Mbf1p and Ribosomal Protein S3: Evidence for Autoregulation of S3 Synthesis. Genetics 157: 1141-1158 [Abstract] [Full Text]  
  • Iouk, T. L., Aitchison, J. D., Maguire, S., Wozniak, R. W. (2001). Rrb1p, a Yeast Nuclear WD-Repeat Protein Involved in the Regulation of Ribosome Biosynthesis. Mol. Cell. Biol. 21: 1260-1271 [Abstract] [Full Text]  
  • WARNER, J.R., VILARDELL, J., SOHN, J.H. (2001). Economics of Ribosome Biosynthesis. Cold Spring Harb Symp Quant Biol 66: 567-574 [Abstract]  
  • Sasaki, T., Toh-e, A., Kikuchi, Y. (2000). Yeast Krr1p Physically and Functionally Interacts with a Novel Essential Kri1p, and Both Proteins Are Required for 40S Ribosome Biogenesis in the Nucleolus. Mol. Cell. Biol. 20: 7971-7979 [Abstract] [Full Text]  
  • Nomura, M. (1999). Regulation of Ribosome Biosynthesis in Escherichia coli and Saccharomyces cerevisiae: Diversity and Common Principles. J. Bacteriol. 181: 6857-6864 [Full Text]  
  • Mariottini, P., Shah, Z. H., Toivonen, J. M., Bagni, C., Spelbrink, J. N., Amaldi, F., Jacobs, H. T. (1999). Expression of the Gene for Mitoribosomal Protein S12 Is Controlled in Human Cells at the Levels of Transcription, RNA Splicing, and Translation. J. Biol. Chem. 274: 31853-31862 [Abstract] [Full Text]