Phosphorylation of Escherichia coli proteins during the SOS response |
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| Institution: | 2. Institut de Biologie Moléculaire et Cellulaire, CNRS, 15 rue René Descartes, 67084 Strasbourg, France;3. Roy J. Carver Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011;4. Molecular, Cellular, and Developmental Biology Interdepartmental Program, Iowa State University, Ames, Iowa 50011;5. Genome Informatics Facility, Office of Biotechnology, Iowa State University, Ames, Iowa 50011;1. Archaeal Biology Center, Institute for Advanced Study, Shenzhen University, Shenzhen 518060, China;2. Shenzhen Key Laboratory of Marine Microbiome Engineering, Institute for Advanced Study, Shenzhen University, Shenzhen 518060, China;1. Mediterranean Institute for Life Sciences (MedILS), 21000 Split, Croatia;2. Inserm Unit 1001, Université Paris-Descartes, Sorbonne Paris Cité, Faculté de Médecine Paris Descartes, 75014 Paris, France;1. School of Biotechnology and Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China;2. State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China;3. 2011 Synergetic Innovation Center of Food Safety and Nutrition, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China;1. Centro de Investigación Médica Aplicada, University of Navarra, Pamplona, Spain;2. Department of Biochemistry and Genetics, University of Navarra, Pamplona, Spain;3. Instituto de Investigación Sanitaria de Navarra, Pamplona, Spain;4. Cancer and Aging Group, Hospital Universitario Virgen de la Arrixaca, and Instituto Murciano de Investigación Biosanitaria, Murcia, Spain;5. Division of Genetic Medicine, Department of Internal Medicine, The University of Michigan Medical School, Ann Arbor, MI;6. Centro de Investigación Biomédica en Red de Oncología, Instituto de Salud Carlos III, Madrid, Spain;7. Hematology Service, Hospital Universitario de Navarra, Pamplona, Spain |
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| Abstract: | - 1.1. The phosphorylation of Escherichia coli proteins was analyzed comparatively before and after induction of the SOS response in a temperature-sensitive mutant strain.
- 2.2. The presence of phosphorylated proteins was evidenced by gel electrophoresis and autoradiography after labelling with radioactive orthophosphate in vivo or radioactive adenosine triphosphate in vitro.
- 3.3. Significant changes in the intensity of protein labelling were observed upon induction of the SOS functions: six proteins were found to be more phosphorylated while two others were less phosphorylated. Moreover, five additional proteins appeared to become phosphorylated exclusively during the SOS response. The molecular mass and isoelectric point of these various proteins were determined.
- 4.4. For most proteins, the changes in the pattern of protein phosphorylation were concomitant with variations in the amount of protein synthesized.
- 5.5. The changes in the pattern of phosphoproteins observed during the SOS response were not due to the temperature shift required experimentally for expressing the SOS phenotype.
- 6.6. Phosphorylation was found to be catalyzed by protein kinases that modify amino acid residues at hydroxyl groups in protein substrates.
- 7.7. Both in vivo and in vitro studies brought evidence that neither RecA nor LexA, the two key regulatory proteins of the SOS functions, were capable of undergoing phosphorylation.
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