When wheat coleoptiles or plants are subjected to a period of heat stress (e.g, at > 35�C for 1 h or more), there is a reduction in normal protein synthesis, accompanied by de novo synthesis of the classical range of heat-shock proteins (based on radioactive tracer experiments) in virtually all parts of the plant. Study of coleoptile elongation rates indicates that this synthesis is related to a protective effect, whereby a preliminary heat shock provides a degree of protection against a later lethal shock. This thermotolerance is also associated with the appearance in coleoptiles and roots of a small peptide (detected without radioactive labelling) whose amino acid sequence (12 residues) is the same as the N-terminal sequence of the alpha- and beta-gliadin proteins of the endosperm.
Heat stress during grain filling leads to important changes in the synthesis of gluten proteins with reduced synthesis of the high molecular weight (HMW) subunits of glutenin, and continuing synthesis of other gluten proteins, particularly various gliadin proteins. This latter group of polypeptides is thus presumed to be acting as heat-shock proteins, and indeed, multiple heat-shock elements are present in the published sequences of representative genes, up-stream of the coding regions.
HPLC analysis (with or without radioactive labelling) shows that there is a resulting change from the normal balance of gluten polypeptides immediately after the shock as well as in the mature grain. As a result, there is a lower proportion of large-sized aggregates of glutenin and weaker dough properties. This scenario indicates that it should be possible to identify genotypes that would be tolerant to stressrelated variations in quality by analysis of gluten composition and, at the gene level, by screening for heat-stress elements in the genes encoding HMW-glutenin subunits. In addition, heat stress modifies the particle size distribution of the starch fraction of mature grain, producing an increase in the proportion of large (A-type) starch granules. No change in chemical structure was detectable as a result of heat stress.
The inhibition of platelet cyclo-oxygenase by aspirin is associated with the acetylation of a 72kDa polypeptide in the intracellular membranes