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Journal of Bacteriology, May 2005, p. 3548-3550, Vol. 187, No. 10
0021-9193/05/$08.00+0     doi:10.1128/JB.187.10.3548-3550.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Severity of the Streptomycin Resistance and Streptomycin Dependence Phenotypes of Ribosomal Protein S12 of Thermus thermophilus Depends on the Identity of Highly Conserved Amino Acid Residues

Jennifer F. Carr, Steven T. Gregory, and Albert E. Dahlberg*

Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, Rhode Island 02912

Received 11 October 2004/ Accepted 14 February 2005

The structural basis for the streptomycin dependence phenotype of ribosomal protein S12 mutants is poorly understood. Here we describe the application of site-directed mutagenesis and gene replacement of Thermus thermophilus rpsL to assess the importance of side chain identity and tertiary interactions as phenotypic determinants of drug-dependent mutants.

* Corresponding author. Mailing address: Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, RI 02912. Phone: (401) 863-2223. Fax: (401) 863-1182. E-mail: Albert_Dahlberg{at}brown.edu.

Journal of Bacteriology, May 2005, p. 3548-3550, Vol. 187, No. 10
0021-9193/05/$08.00+0     doi:10.1128/JB.187.10.3548-3550.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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