Stoichiometry of Sulfolobus ribosomal protein L12e in 50S subunits determined by quantification of immunoblots.
A monoclonal antibody reactive with Sulfolobus solfataricus acidic ribosomal protein SsoL12e was prepared and employed to determine the stoichiometry of this protein in 50S ribosomal subunits by quantification of chloronaphthol-stained protein bands from immunoblots. Approximately four copies of SsoL12e were detected per 50S ribosome. This finding extends previous studies demonstrating the involvement of this protein in a multimeric protein complex in the ribosomal factor binding domain of Sulfolobus and strengthens the concept that this structural motif is a highly conserved and presumably critical feature of the ribosome.
Casiano
C A
CA
Department of Biological Chemistry, School of Medicine, University of California, Davis 95616.
Traut
R R
RR
D000911:Antibodies, Monoclonal; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000737:chemistry; D029968:Escherichia coli Proteins; D015151:Immunoblotting; D012269:Ribosomal Proteins / Q000032:analysis / Q000737:chemistry*; D012270:Ribosomes / Q000737:chemistry; D016944:Sulfolobus / Q000737:chemistry*
D000911:Antibodies, Monoclonal; D029968:Escherichia coli Proteins; D012269:Ribosomal Proteins; C512844:rplL protein, E coli