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...

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Bibliographic Details
Published in:FEMS Microbiology Letters
Main Authors: Ray, M.K., Seshu Kumar, G., Shivaji, S.
Format: Text
Language:English
Published: Oxford University Press 1994
Subjects:
Articles
Antarctic
The Antarctic
Triton
Antarc*
Online Access:http://femsle.oxfordjournals.org/cgi/content/short/122/1-2/49
https://doi.org/10.1111/j.1574-6968.1994.tb07142.x
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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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