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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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Identification of the 50S Ribosomal Proteins from the Eubacterium Thermus thermophilus

K.R. Katsani / P. Tsiboli / K. Anagnostopoulos / H. Urlaub / T. Choli-Papadopoulou

Citation Information: Biological Chemistry. Volume 381, Issue 11, Pages 1079–1087, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2000.133, July 2005

Publication History

Published Online:


The total protein mixture from the 50S subunit (TP-50) of the eubacterium Thermus thermophilus was characterized after blotting onto PVDF membranes from two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) and sequencing. The proteins were numbered according to their primary structure similarity with their counterparts from other species. One of them has been marked with an asterisk, namely L*23, because unlike the other known ribosomal proteins it shows a very low degree of homology.

A highly acidic 5S rRNA binding protein, TL5, was characterized and compared with the available primary structure information.

Proteins L1 and L4 migrate similarly on 2D-PAGE. Protein L4, essential for protein biosynthesis, is N-terminally blocked and shows a strikingly low homology to other L4 proteins. In addition to L4, two other proteins, namely L10 and L11, were found to be N-terminally blocked.

In conclusion, 33 proteins from the large subunit were identified, including TL5. Homologs to rpL25 and rpL26 were not found.

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D. Triantafillidou, E. Persidou, D. Lazarou, P. Andrikopoulos, F. Leontiadou, and T. Choli-Papadopoulou
Biological Chemistry, 2004, Volume 385, Number 1

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