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 Pfister, P.
Right arrow Articles by Böttger, E. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pfister, P.
Right arrow Articles by Böttger, E. C.

 Previous Article  |  Next Article 

Antimicrobial Agents and Chemotherapy, May 2003, p. 1496-1502, Vol. 47, No. 5
0066-4804/03/$08.00+0     DOI: 10.1128/AAC.47.5.1496-1502.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Role of 16S rRNA Helix 44 in Ribosomal Resistance to Hygromycin B

P. Pfister,1 M. Risch,1 D. E. Brodersen,2 and E. C. Böttger1*

Institut für Medizinische Mikrobiologie, Universität Zürich, CH-8028 Zürich, Switzerland,1 MRC Laboratory of Molecular Biology, Cambridge CB2 2QH, United Kingdom2

Received 22 November 2002/ Returned for modification 6 January 2003/ Accepted 3 February 2003

Hygromycin B is an aminoglycoside antibiotic active against prokaryotic and eukaryotic ribosomes. Ribosomal alterations in bacteria conferring resistance to hygromycin B have not been described, prompting us to use a single rRNA allelic derivative of the gram-positive bacterium Mycobacterium smegmatis for investigation of the molecular mechanisms involved in ribosomal resistance to hygromycin B in eubacteria. Resistance mutations were found to localize exclusively in 16S rRNA. The mutations observed, i.e., 16S rRNA U1406C, C1496U, and U1498C (E. coli numbering), are in close proximity to the hygromycin B binding site located in conserved helix 44 of 16S rRNA. The 16S rRNA positions involved in hygromycin B resistance are highly conserved in all three domains of life, explaining the lack of specificity and general toxicity of hygromycin B.


* Corresponding author. Mailing address: Institut für Medizinische Mikrobiologie, Universität Zürich, Gloriastr. 30/32, CH-8028 Zürich, Switzerland. Phone: 41-1-634 26 60/61. Fax: 41-1-634 49 06. E-mail: boettger{at}immv.unizh.ch.


Antimicrobial Agents and Chemotherapy, May 2003, p. 1496-1502, Vol. 47, No. 5
0066-4804/03/$08.00+0     DOI: 10.1128/AAC.47.5.1496-1502.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Borovinskaya, M. A., Shoji, S., Fredrick, K., Cate, J. H.D. (2008). Structural basis for hygromycin B inhibition of protein biosynthesis. RNA 14: 1590-1599 [Abstract] [Full Text]  
  • Liu, M., Zhang, Y., Inouye, M., Woychik, N. A. (2008). Bacterial addiction module toxin Doc inhibits translation elongation through its association with the 30S ribosomal subunit. Proc. Natl. Acad. Sci. USA 105: 5885-5890 [Abstract] [Full Text]  
  • Haiser, H. J., Karginov, F. V., Hannon, G. J., Elliot, M. A. (2008). Developmentally regulated cleavage of tRNAs in the bacterium Streptomyces coelicolor. Nucleic Acids Res 36: 732-741 [Abstract] [Full Text]  
  • Fan-Minogue, H., Bedwell, D. M. (2008). Eukaryotic ribosomal RNA determinants of aminoglycoside resistance and their role in translational fidelity. RNA 14: 148-157 [Abstract] [Full Text]  
  • Hobbie, S. N., Pfister, P., Bruell, C., Sander, P., Francois, B., Westhof, E., Bottger, E. C. (2006). Binding of Neomycin-Class Aminoglycoside Antibiotics to Mutant Ribosomes with Alterations in the A Site of 16S rRNA.. Antimicrob. Agents Chemother. 50: 1489-1496 [Abstract] [Full Text]  
  • Hobbie, S. N., Pfister, P., Brull, C., Westhof, E., Bottger, E. C. (2005). Analysis of the Contribution of Individual Substituents in 4,6-Aminoglycoside-Ribosome Interaction. Antimicrob. Agents Chemother. 49: 5112-5118 [Abstract] [Full Text]  
  • Mathis, A., Wild, P., Boettger, E. C., Kapel, C. M. O., Deplazes, P. (2005). Mitochondrial Ribosome as the Target for the Macrolide Antibiotic Clarithromycin in the Helminth Echinococcus multilocularis. Antimicrob. Agents Chemother. 49: 3251-3255 [Abstract] [Full Text]  
  • Gregory, S. T., Carr, J. F., Rodriguez-Correa, D., Dahlberg, A. E. (2005). Mutational Analysis of 16S and 23S rRNA Genes of Thermus thermophilus. J. Bacteriol. 187: 4804-4812 [Abstract] [Full Text]  
  • Binet, R., Maurelli, A. T. (2005). Frequency of Spontaneous Mutations That Confer Antibiotic Resistance in Chlamydia spp.. Antimicrob. Agents Chemother. 49: 2865-2873 [Abstract] [Full Text]  
  • Pfister, P., Corti, N., Hobbie, S., Bruell, C., Zarivach, R., Yonath, A., Bottger, E. C. (2005). 23S rRNA base pair 2057-2611 determines ketolide susceptibility and fitness cost of the macrolide resistance mutation 2058A->G. Proc. Natl. Acad. Sci. USA 102: 5180-5185 [Abstract] [Full Text]  
  • Poehlsgaard, J., Pfister, P., Bottger, E. C., Douthwaite, S. (2005). Molecular Mechanisms by Which rRNA Mutations Confer Resistance to Clindamycin. Antimicrob. Agents Chemother. 49: 1553-1555 [Abstract] [Full Text]  
  • Clarridge, J. E. III (2004). Impact of 16S rRNA Gene Sequence Analysis for Identification of Bacteria on Clinical Microbiology and Infectious Diseases. Clin. Microbiol. Rev. 17: 840-862 [Abstract] [Full Text]