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Covalent modification of proteins in Bacillus subtilis during the process of sporulation, germination and outgrowth
Author(s) -
Köhler E.,
Antranikian G.
Publication year - 1989
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1989.tb03226.x
Subject(s) - bacillus subtilis , phosphorylation , biochemistry , germination , spore , gel electrophoresis , molecular mass , posttranslational modification , protein phosphorylation , spore germination , biology , electrophoresis , chemistry , kinase , protein kinase a , microbiology and biotechnology , enzyme , bacteria , botany , genetics
Cells of Bacillus subtilis 168 + were labeled with 32 P‐orthophosphate during the process of sporulation, germination and outgrowth. By two‐dimensional gel electrophoresis, at least 30 protein species were found to be radioactively labeled; 30% of these were modified by phosphorylation. Significant changes in the protein phosphorylation pattern during growth and cellular differentiation could be demonstrated. Using γ‐ 32 P‐ATP evidence for an ATP‐dependent protein kinase was also obtained. Under these conditions 4 proteins with a molecular mass of 109 600; 103 100; 73 300 and 32 200 Da were found to be phosphorylated.