Characterization and primary structure of proteins L28, L33 and L34 from Bacillus stearothermophilus ribosomes.
The complete amino acid sequences of 3 proteins from the 50S subunit of Bacillus stearothermophilus ribosomes were determined by N-terminal sequence analysis and by sequencing of overlapping fragments obtained from enzymatic digestions and chemical cleavages. The proteins BstL28, BstL33 and BstL34, named according to the equivalent proteins in Escherichia coli ribosomes, consist of 60, 49, and 44 amino acid residues and have calculated molecular masses of 6811.0, 5908.6, and 5253.9 Da, respectively. They are highly basic with a content of positively charged residues ranging between 29% for L33 and 45% for L34. The 3 proteins were positioned in the 2-dimensional map of B stearothermophilus 50S ribosomal proteins. The electrophoretic mobilities confirm sizes and net charges deduced from the sequences.
Kruft
V
V
Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, Berlin, Germany.
Kapp
U
U
Wittmann-Liebold
B
B
D000595:Amino Acid Sequence; D000814:Aniline Compounds; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics; D029968:Escherichia coli Proteins; D001411:Geobacillus stearothermophilus / Q000235:genetics*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011487:Protein Conformation; D012269:Ribosomal Proteins / Q000737:chemistry / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid
D000814:Aniline Compounds; D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C489050:L33 ribosomal protein, bacteria; D012269:Ribosomal Proteins; C041672:ribosomal protein L34; C489322:rpmB protein, E coli; C489052:rpmG protein, E coli; C487557:4-trifluoromethylaniline