Heat shock and deciliation induce phosphorylation of histone H1 in T. pyriformis.
Both heat shock and decilliation of Tetrahymena pyriformis lead to an increase in the level of histone H1 phosphorylation. After heat shock, starved or growing cells reach the same maximum level of H1 phosphorylation, although the increase is more easily detected in starved cells because of their relatively low initial level of phosphorylation. In starved cells, stress-induced phosphorylation is rapid, involves a large percentage of the H1, occurs at multiple sites on the H1 molecule and is inhibited by cycloheximide. Stress-induced phosphorylation of H1 in Tetrahymena thus has many properties in common with cell-cycle-dependent H1 phosphorylation although it is not coupled to the cell cycle.
D000818:Animals; D002923:Cilia / Q000502:physiology*; D004591:Electrophoresis, Polyacrylamide Gel; D005786:Gene Expression Regulation; D006657:Histones / Q000378:metabolism*; D006358:Hot Temperature; D007700:Kinetics; D010766:Phosphorylation; D006656:Protamine Kinase / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism*; D013769:Tetrahymena pyriformis / Q000502:physiology*
D006657:Histones; D011494:Protein Kinases; D006656:Protamine Kinase