Cross-linking studies on the 50 S ribosomal subunit of Escherichia coli with methyl 4-mercaptobutyrimidate.
The 50 S ribosomal subunits of Escherichia coli were incubated with methyl 4-mercaptobutyrimidate and the formation of intermolecular protein:protein disulfide bonds was promoted by oxidation. Cross-linked proteins were analyzed by diagonal polyacrylamide/sodium dodecyl sulfate gel electrophoresis. Three pairs of cross-linked proteins were identified: L2-L7,L12; L5-L7,L12; and L17-L32. The significance of the results in relation to the location of sites for factor binding, peptidyltransferase, and GTP hydrolysis is discussed.
D002087:Butyrates; D004926:Escherichia coli / Q000648:ultrastructure*; D007096:Imidoesters; D007097:Imines; D046911:Macromolecular Substances; D008970:Molecular Weight; D011485:Protein Binding; D012269:Ribosomal Proteins / Q000032:analysis*; D012270:Ribosomes / Q000648:ultrastructure*
D002087:Butyrates; D007096:Imidoesters; D007097:Imines; D046911:Macromolecular Substances; D012269:Ribosomal Proteins; C005905:methyl 4-mercaptobutyrimidate