Effect of heat shock on S6 phosphorylation during the development of Blastocladiella emersonii.
Changes in phosphorylation of ribosomal protein S6 during heat shock, induction of thermotolerance and recovery from heat shock at different stages of Blastocladiella emersonii development were investigated. Independently of the initial state of S6 phosphorylation (maximal or intermediate), a rapid and complete dephosphorylation of S6 is induced by heat shock and S6 remains unphosphorylated during the acquired thermotolerance. During recovery from heat shock rephosphorylation of S6 occurs always to the levels characteristic of that particular stage, coincidently with the turn off of heat shock protein synthesis.
da Silva
A M
AM
Departamento de Bioquímica, Universidade de São Paulo, Brasil.
Juliani
M H
MH
Bonato
M C
MC
D000818:Animals; D001754:Blastocladiella / Q000254:growth & development / Q000378:metabolism*; D002478:Cells, Cultured; D008411:Chytridiomycota / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005658:Fungi / Q000254:growth & development / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000378:metabolism*; D010766:Phosphorylation; D038601:Ribosomal Protein S6; D012269:Ribosomal Proteins / Q000378:metabolism*
D006360:Heat-Shock Proteins; D038601:Ribosomal Protein S6; D012269:Ribosomal Proteins