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

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

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.

Biological Chemistry, Walter de Gruyter

Print ISSN: 1431-6730
Volume: 381, 11/2000
Pages: 1079 - 1087

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