Heat shock triggers rapid protein phosphorylation in soybean seedings.
Heat shock arrests the synthesis of many cellular proteins and simultaneously initiates expression of a unique set of proteins, termed heat shock proteins. We have found that heat shock rapidly triggers phosphorylation of a set of proteins in soybean seedlings. Although the kinetics of phosphorylation and the heat shock response are similar, the major identified phosphorylation products do not comigrate with heat shock proteins on polyacrylamide gels. Cadmium, which is known to induce the heat shock response, stimulates phosphorylation of the same set of proteins. The rapidity of phosphorylation suggests that it may play a pivotal role in sensing and transducing elevated temperature stress in plants.
Department of Plant Pathology, University of Missouri, Columbia 65211.
H B
HB
Krishnan
S G
SG
Pueppke
D002104:Cadmium / Q000494:pharmacology; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006358:Hot Temperature; D010710:Phosphates / Q000378:metabolism; D010750:Phosphoproteins / Q000096:biosynthesis* / Q000302:isolation & purification; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D010944:Plants / Q000378:metabolism*; D014176:Protein Biosynthesis; D013025:Glycine max
D006360:Heat-Shock Proteins; D010710:Phosphates; D010750:Phosphoproteins; D010761:Phosphorus Radioisotopes; D010940:Plant Proteins; D002104:Cadmium