Phosphorylation of GroEL, DnaK and other proteins from Thiobacillus ferrooxidans grown under different conditions.
The levels of phosphorylation of the chaperones DnaK and GroEL and other proteins varied when cells of Thiobacillus ferrooxidans were subjected to phosphate starvation. The phosphorylated amino acid of GroEL was found to be threonine. Our results show that not only heat shock, but also a nutrient starvation stress leads to phosphorylation of chaperones and, in addition, support the possible role of phosphorylation of these proteins in the sensing and regulation of stress responses in bacteria.
Seeger
M
M
Departamento de Bioquímica, Facultad de Medicina, Universidad de Chile, Santiago, Chile.
Osorio
G
G
Jerez
C A
CA
D001426:Bacterial Proteins / Q000378:metabolism*; D018834:Chaperonin 60 / Q000378:metabolism*; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D010710:Phosphates / Q000378:metabolism; D010766:Phosphorylation; D013855:Thiobacillus / Q000254:growth & development / Q000378:metabolism*; D013912:Threonine / Q000378:metabolism
D001426:Bacterial Proteins; D018834:Chaperonin 60; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D010710:Phosphates; D013912:Threonine; C063842:dnaK protein, E coli