Tyrosine phosphorylation of a cytoplasmic protein from the antarctic psychrotrophic bacterium Pseudomonas syringae

Ray, M. K. ; Seshu Kumar, G. ; Shivaji, S. (1994) Tyrosine phosphorylation of a cytoplasmic protein from the antarctic psychrotrophic bacterium Pseudomonas syringae FEMS Microbiology Letters, 122 (1-2). pp. 49-54. ISSN 0378-1097

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Official URL: http://onlinelibrary.wiley.com/doi/10.1111/j.1574-...

Related URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb07142.x

Abstract

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.

Item Type:Article
Source:Copyright of this article belongs to John Wiley and Sons.
Keywords:Tyrosine Phosphorylation; Psychrotroph; Antarctica; Pseudomonas syringae
ID Code:64327
Deposited On:07 Oct 2011 12:37
Last Modified:07 Oct 2011 12:37

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