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Evidence for protein phosphorylation inStreptomyces lincolnensis

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Abstract

Protein phosphorylation was investigated inStreptomyces lincolnensis underin vivo conditions. In cells grown in the presence of32P-orthophosphate, proteins ofM=12, 22, 45, 68 and 90 kDa were labeled with32P (detected by gel electrophoresis and autoradiography). These proteins were shown to contain O-phosphoserine and a small proportion of O-phosphotyrosine. Taken together the results indicate thatStreptomyces lincolnensis harbors several protein kinases including a protein-tyrosine kinase activity.

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Authors and Affiliations

  1. Laboratory of Biochemistry and Genetics of Cellular Regulations, Institute of Microbiology, Academy of Sciences of the Czech Republic, 142 20, Prague 4

    J. Janeček, Z. Dobrová, J. Náprstek, P. Ryšavý & V. Moravec

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  1. J. Janeček
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  2. Z. Dobrová
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  3. J. Náprstek
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  4. P. Ryšavý
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  5. V. Moravec
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Janeček, J., Dobrová, Z., Náprstek, J. et al. Evidence for protein phosphorylation inStreptomyces lincolnensis . Folia Microbiol 40, 249–252 (1995). https://doi.org/10.1007/BF02814201

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  • DOI: https://doi.org/10.1007/BF02814201

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