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.
Katsani
K R
KR
Laboratory of Biochemistry, School of Chemistry, Aristotle University of Thessaloniki, Greece.
Tsiboli
P
P
Anagnostopoulos
K
K
Urlaub
H
H
Choli-Papadopoulou
T
T
D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000032:analysis* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D012269:Ribosomal Proteins / Q000032:analysis* / Q000302:isolation & purification; D012270:Ribosomes / Q000737:chemistry; D016963:Thermus thermophilus / Q000737:chemistry*
D001426:Bacterial Proteins; D012269:Ribosomal Proteins