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 Lin, B.
Right arrow Articles by Maddock, J. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lin, B.
Right arrow Articles by Maddock, J. R.

 Previous Article  |  Next Article 

Journal of Bacteriology, January 2004, p. 481-489, Vol. 186, No. 2
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.2.481-489.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

The Caulobacter crescentus CgtAC Protein Cosediments with the Free 50S Ribosomal Subunit

Bin Lin, Desiree A. Thayer, and Janine R. Maddock*

Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109

Received 23 June 2003/ Accepted 10 October 2003

The Obg family of GTPases is widely conserved and predicted to play an as-yet-unknown role in translation. Recent reports provide circumstantial evidence that both eukaryotic and prokaryotic Obg proteins are associated with the large ribosomal subunit. Here we provide direct evidence that the Caulobacter crescentus CgtAC protein is associated with the free large (50S) ribosomal subunit but not with 70S monosomes or with translating ribosomes. In contrast to the Bacillus subtilis and Escherichia coli proteins, CgtAC does not fractionate in a large complex by gel filtration, indicating a moderately weak association with the 50S subunit. Moreover, binding of CgtAC to the 50S particle is sensitive to salt concentration and buffer composition but not guanine nucleotide occupancy of CgtAC. Assays of epitope-tagged wild-type and mutant variants of CgtAC indicate that the C terminus of CgtAC is critical for 50S association. Interestingly, the addition of a C-terminal epitope tag also affected the ability of various cgtAC alleles to function in vivo. Depletion of CgtAC led to perturbations in the polysome profile, raising the possibility that CgtAC is involved in ribosome assembly or stability.

* Corresponding author. Mailing address: Department of Molecular, Cellular and Developmental Biology, University of Michigan, 830 North University, Ann Arbor, MI 48109-1048. Phone: (734) 936-8068. Fax: (734) 647-0884. E-mail: maddock{at}umich.edu.

{dagger} Present address: NABI Biopharmaceuticals, Rockville, MD 20852.

Journal of Bacteriology, January 2004, p. 481-489, Vol. 186, No. 2
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.2.481-489.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Wout, P. K., Sattlegger, E., Sullivan, S. M., Maddock, J. R. (2009). Saccharomyces cerevisiae Rbg1 Protein and Its Binding Partner Gir2 Interact on Polyribosomes with Gcn1. Eukaryot Cell 8: 1061-1071 [Abstract] [Full Text]  
  • Polkinghorne, A., Ziegler, U., Gonzalez-Hernandez, Y., Pospischil, A., Timms, P., Vaughan, L. (2008). Chlamydophila pneumoniae HflX belongs to an uncharacterized family of conserved GTPases and associates with the Escherichia coli 50S large ribosomal subunit. Microbiology 154: 3537-3546 [Abstract] [Full Text]  
  • Kuo, S., Demeler, B., Haldenwang, W. G. (2008). The Growth-Promoting and Stress Response Activities of the Bacillus subtilis GTP Binding Protein Obg Are Separable by Mutation. J. Bacteriol. 190: 6625-6635 [Abstract] [Full Text]  
  • Wicker-Planquart, C., Foucher, A.-E., Louwagie, M., Britton, R. A., Jault, J.-M. (2008). Interactions of an Essential Bacillus subtilis GTPase, YsxC, with Ribosomes. J. Bacteriol. 190: 681-690 [Abstract] [Full Text]  
  • Lapik, Y. R., Misra, J. M., Lau, L. F., Pestov, D. G. (2007). Restricting Conformational Flexibility of the Switch II Region Creates a Dominant-Inhibitory Phenotype in Obg GTPase Nog1. Mol. Cell. Biol. 27: 7735-7744 [Abstract] [Full Text]  
  • Jiang, M., Sullivan, S. M., Wout, P. K., Maddock, J. R. (2007). G-Protein Control of the Ribosome-Associated Stress Response Protein SpoT. J. Bacteriol. 189: 6140-6147 [Abstract] [Full Text]  
  • Matsuo, Y., Oshima, T., Loh, P. C., Morimoto, T., Ogasawara, N. (2007). Isolation and Characterization of a Dominant Negative Mutant of Bacillus subtilis GTP-binding Protein, YlqF, Essential for Biogenesis and Maintenance of the 50 S Ribosomal Subunit. J. Biol. Chem. 282: 25270-25277 [Abstract] [Full Text]  
  • Jiang, M., Sullivan, S. M., Walker, A. K., Strahler, J. R., Andrews, P. C., Maddock, J. R. (2007). Identification of Novel Escherichia coli Ribosome-Associated Proteins Using Isobaric Tags and Multidimensional Protein Identification Techniques. J. Bacteriol. 189: 3434-3444 [Abstract] [Full Text]  
  • Raskin, D. M., Judson, N., Mekalanos, J. J. (2007). Regulation of the stringent response is the essential function of the conserved bacterial G protein CgtA in Vibrio cholerae. Proc. Natl. Acad. Sci. USA 104: 4636-4641 [Abstract] [Full Text]  
  • Schaefer, L., Uicker, W. C., Wicker-Planquart, C., Foucher, A.-E., Jault, J.-M., Britton, R. A. (2006). Multiple GTPases Participate in the Assembly of the Large Ribosomal Subunit in Bacillus subtilis. J. Bacteriol. 188: 8252-8258 [Abstract] [Full Text]  
  • Bharat, A., Jiang, M., Sullivan, S. M., Maddock, J. R., Brown, E. D. (2006). Cooperative and Critical Roles for Both G Domains in the GTPase Activity and Cellular Function of Ribosome-Associated Escherichia coli EngA. J. Bacteriol. 188: 7992-7996 [Abstract] [Full Text]  
  • Hirano, Y., Ohniwa, R. L., Wada, C., Yoshimura, S. H., Takeyasu, K. (2006). Human small G proteins, ObgH1, and ObgH2, participate in the maintenance of mitochondria and nucleolar architectures. GENES CELLS 11: 1295-1304 [Abstract] [Full Text]  
  • Jiang, M., Datta, K., Walker, A., Strahler, J., Bagamasbad, P., Andrews, P. C., Maddock, J. R. (2006). The Escherichia coli GTPase CgtAE Is Involved in Late Steps of Large Ribosome Assembly.. J. Bacteriol. 188: 6757-6770 [Abstract] [Full Text]  
  • Sikora, A. E., Zielke, R., Datta, K., Maddock, J. R. (2006). The Vibrio harveyi GTPase CgtAV Is Essential and Is Associated with the 50S Ribosomal Subunit. J. Bacteriol. 188: 1205-1210 [Abstract] [Full Text]  
  • Sato, A., Kobayashi, G., Hayashi, H., Yoshida, H., Wada, A., Maeda, M., Hiraga, S., Takeyasu, K., Wada, C. (2005). The GTP binding protein Obg homolog ObgE is involved in ribosome maturation. GENES CELLS 10: 393-408 [Abstract] [Full Text]  
  • Datta, K., Fuentes, J. L., Maddock, J. R. (2005). The Yeast GTPase Mtg2p Is Required for Mitochondrial Translation and Partially Suppresses an rRNA Methyltransferase Mutant, mrm2. Mol. Biol. Cell 16: 954-963 [Abstract] [Full Text]  
  • Wout, P., Pu, K., Sullivan, S. M., Reese, V., Zhou, S., Lin, B., Maddock, J. R. (2004). The Escherichia coli GTPase CgtAE Cofractionates with the 50S Ribosomal Subunit and Interacts with SpoT, a ppGpp Synthetase/Hydrolase. J. Bacteriol. 186: 5249-5257 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»