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Published online 11 May 2004

Nucleic Acids Research, 2004, Vol. 32, No. 8 2594-2597
© 2004 Oxford University Press

Mapping of the second tetracycline binding site on the ribosomal small subunit of E.coli

Maria M. Anokhina1, Andrea Barta2, Knud H. Nierhaus3, Vera A. Spiridonova4 and Alexei M. Kopylov*,1,4

1 Department of Chemistry, Moscow State University, 119992 Moscow, Russian Federation, 2 Institute of Biochemistry, University of Vienna, Vienna Biocenter, A1030 Vienna, Austria, 3 Max-Planck Institute for Molecular Genetics, D-14195 Berlin-Dahlem, Germany and 4 A.N. Belozersky Institute of Physical Chemical Biology, Moscow State University, 119992 Moscow, Russian Federation

*To whom correspondence should be addressed. Tel: +7 095 939 3143; Fax: +7 095 939 3181; Email: kopylov{at}rnp-group.genebee.msu.su

Received February 5, 2004; Revised March 22, 2004; Accepted April 14, 2004

Tetracycline blocks stable binding of aminoacyl-tRNA to the bacterial ribosomal A-site. Various tetracycline binding sites have been identified in crystals of the 30S ribosomal small subunit of Thermus thermophilus. Here we describe a direct photo- affinity modification of the ribosomal small subunits of Escherichia coli with 7-[3H]-tetracycline. To select for specific interactions, an excess of the 30S subunits over tetracycline has been used. Primer extension analysis of the 16S rRNA revealed two sites of the modifications: C936 and C948. Considering available data on tetracycline interactions with the prokaryotic 30S subunits, including the presented data (E.coli), X-ray data (T.thermophilus) and genetic data (Helicobacter pylori, E.coli), a second high affinity tetracycline binding site is proposed within the 3'-major domain of the 16S rRNA, in addition to the A-site related tetracycline binding site.


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