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Protein Synthesis in the Isolated Forespores from Sporulating Cells of Bacillus subtilis
Author(s) -
Watabe Kazuhito,
Iida Seiichi,
Nakamura Keiko,
Ichikawa Tomio,
Kondo Masaomi
Publication year - 1981
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1981.tb00056.x
Subject(s) - bacillus subtilis , biology , cytoplasm , gel electrophoresis , biochemistry , sodium dodecyl sulfate , spore , molecular mass , fractionation , polyacrylamide gel electrophoresis , amino acid , cell fractionation , protein biosynthesis , phenylalanine , microbiology and biotechnology , chromatography , bacteria , enzyme , chemistry , genetics
Developing forespores were isolated from Bacillus subtilis at different stages of sporulation and protein synthesis in the forespore compartment was examined. Pulse‐labeling experiments indicated that [ 14 C]phenylalanine was continuously incorporated into the sporangium throughout sporulation, and at t 5 (early stage V of sporulation) 58% of the radioactivity was located in the forespore compartment. Significantly high incorporation of [ 14 C]phenylalanine was observed when the isolated forespores at t 5 were incubated with the corresponding mother‐cell cytoplasmic fraction or an amino acid mixture. About 73% of the radioactivity incorporated into the isolated forespore at t 5 was found in the cytoplasmic fraction and 26% in the membranous fraction. Analysis by sodium dodecyl sulfate‐gel electrophoresis showed that the 14 C‐labeled cytoplasmic protein had a molecular weight of about 20,000, and that a protein having the same molecular weight was present in the t 5 forespore as a slight protein band and also in the mature spore as a clear protein band. Gel electrophoresis also revealed that the 14 C‐labeled membranous‐soluble protein (prepared by solubilization with detergents) had broad peaks with molecular weights of about 74,000, 33,000, 20,000, and 12,000.

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