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Identification of the 50S Ribosomal Proteins from the Eubacterium Thermus thermophilus
Citation Information: Biological Chemistry. Volume 381, Issue 11, Pages 1079–1087, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2000.133, July 2005
- 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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