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Volume 271, Number 51, Issue of December 20, 1996 pp. 32849-32856
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Mutational Analysis of Two Highly Conserved UGG Sequences of 23 S rRNA from Escherichia coli

(Received for publication, July 2, 1996, and in revised form, September 12, 1996)

Christian M. T. Spahn , Jaanus Remme ^§ , Markus A. Schäfer and Knud H. Nierhaus

From the  Max-Planck-Institut für Molekulare Genetik, AG Ribosomen, Ihnestrasse 73, D-14195 Berlin, Germany and the ^§ Institute of Molecular and Cell Biology, Tartu University, Riia 23, EE-2400 Tartu, Estonia

The 23 S-type rRNA contains two phylogenetically conserved UGG sequences, which have the potential to bind the universal CCA-3-ends of tRNAs at the ribosomal peptidyltransferase center by base pairing. The first two positions, UG, of these sequences at the helix-loop 80 (U2249G2250) and helix-loop 90 (2580G2581) and some related nucleotides were tested by site-directed mutagenesis for their involvement in ribosomal function, i.e. peptidyltransferase. The plasmid-derived mutated 23 S rRNA comprised about 50% of the total 23 S rRNA. None of the single mutations caused an assembly defect, and all 50 S subunits carrying an altered 23 S rRNA could freely exchange with the pools of 70S ribosomes and polysomes. The mutations at the helix-loop 80 region hardly affected bacterial growth. However, mutations at the helix 90 caused severe growth effects and severely impaired the in vitro protein synthesis, showing that this 23 S rRNA region is of high importance for ribosomal function.

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