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Journal of Bacteriology logoLink to Journal of Bacteriology
. 1989 Jan;171(1):272–279. doi: 10.1128/jb.171.1.272-279.1989

Nucleotidylation, not phosphorylation, is the major source of the phosphotyrosine detected in enteric bacteria.

R Foster 1, J Thorner 1, G S Martin 1
PMCID: PMC209582  PMID: 2464577

Abstract

The majority of the phosphotyrosine recovered from partial acid hydrolysates of 32P-labeled Escherichia coli is derived from a single prominent protein. We show here by biochemical, genetic, and immunological criteria that this protein is actually glutamine synthetase adenylylated (not phosphorylated) at tyrosine. Furthermore, all of the phosphotyrosine detectable in partial acid hydrolysates of 32P-labeled Salmonella typhimurium was eliminated in a strain deficient in both glutamine synthetase and uridylyltransferase, an enzyme which uridylylates the regulatory protein PII at a tyrosine residue. These results suggest that protein-tyrosine phosphorylation represents a rare modification in eubacterial cells.

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Selected References

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