Analysis of bacterial biotin-proteins.
The biotin-protein populations in several bacterial strains were analyzed by solubilization of [3H]biotin-labeled cells with sodium dodecylsulfate followed by electrophoresis on polyacrylamide gels containing the detergent. A variety of patterns of biotin-labeled polypeptide chains was seen, ranging from a single biotin-protein in Escherichia coli, corresponding to the biotin carboxyl carrier protein component of acetyl-CoA carboxylase, to multiple species in Enterobacter aerogenes, Pseudomonas citronellolis, Bacillus cereus, Propionibacterium shermanii, Lactobacillus plantarum, and Mycobacterium phlei, which probably represent subunits of multiple biotin-dependent enzymes present in these organisms. In the case of Pseudomonas citronellolis two major biotin-containing polypeptides with approximate molecular weights of 65 000 and 25 000 were shown to correspond to the biotin carboxyl carrier components of pyruvate carboxylase and acetyl-CoA carboxylase, respectively. Thus in the case of Pseudomonas citronellolis two different biotin-dependent enzymes in the same cell do not share common biotin carboxyl carrier subunits.
D000103:Acetyl-CoA Carboxylase / Q000032:analysis; D001409:Bacillus cereus / Q000032:analysis; D001426:Bacterial Proteins; D001710:Biotin / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D004755:Enterobacteriaceae / Q000032:analysis; D007778:Lactobacillus / Q000032:analysis; D008970:Molecular Weight; D009161:Mycobacterium / Q000032:analysis; D011424:Propionibacterium / Q000032:analysis; D011549:Pseudomonas / Q000032:analysis / Q000201:enzymology; D011766:Pyruvate Carboxylase / Q000032:analysis; D013045:Species Specificity
D001426:Bacterial Proteins; D001710:Biotin; D011766:Pyruvate Carboxylase; D000103:Acetyl-CoA Carboxylase