1998 Volume 12 Issue 2 Pages 65-70
Proteome analysis of the membrane proteins from Streptomyces coelicolor A3 (2) was carried out. By two-dimensional polyacrylamide gel electrophoresis, over 100 protein spots were detected by Coomassie staining. Among them, nine proteins gave clear amino acid sequences after digestion with trypsin or lysylendopeptidase followed by the separation on HPLC and sequence analyses. Homology analyses of the peptides indicate that protein numbers 1, 2, 3, 4, 5 and 6 are AtpD, AtpA, GroEL2, GroELl, BldKB and BldKB, respectively. Proteins 5 and 6 are supposed to the same proteins with different modification or isoproteins. However, sequence analyses of the peptides from protein numbers 7, 8, and 9 gave no information about homologous proteins. It is suggested, therefore, that some major proteins in a large amount of protein in the membrane have their characteristic functions in the membrane of Streptomyces coelicolor A3(2), which are not known in other eubacteria.