Tyrosine phosphorylation of a cytoplasmic protein from the antarctic psychrotrophic bacterium Pseudomonas syringae
Cytoplasmic proteins from the antarctic psychrotrophic bacterium Pseudomonas syringae showed two phosphorylated proteins of molecular mass 66 kDa and 62 kDa. The phosphorylation of 66 kDa protein was enhanced in the presence of Triton X-100 solubilised membrane proteins at a higher temperature (30°C...
| Main Authors: | , , |
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| Format: | Article in Journal/Newspaper |
| Language: | unknown |
| Published: |
John Wiley and Sons
1994
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| Subjects: | |
| Online Access: | http://repository.ias.ac.in/64327/ http://onlinelibrary.wiley.com/doi/10.1111/j.1574-6968.1994.tb07142.x/abstract |
| Summary: | Cytoplasmic proteins from the antarctic psychrotrophic bacterium Pseudomonas syringae showed two phosphorylated proteins of molecular mass 66 kDa and 62 kDa. The phosphorylation of 66 kDa protein was enhanced in the presence of Triton X-100 solubilised membrane proteins at a higher temperature (30°C) only. Western blot analysis and phosphoamino acid analysis indicated that the 66 kDa protein is phosphorylated at a tyrosine residue. Surprisingly, sodium orthovanadate, which is a known phosphotyrosine phosphatase (PTPase) inhibitor, inhibited the phosphorylation of the protein. The possible importance of this tyrosine phosphorylated protein to growth at low temperature is suggested. |
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