Translational efficiency of wheat ribosomes was studied as a function
of an in vivo temperature pretreatment of wheat seedlings. The ribosom
es were isolated from 41 or 36-degrees-C-adapted and non-adapted (20-d
egrees-C) wheat seedlings. The poly-U-dependent translational efficien
cy, measured as H-3 phenylalanine incorporation into poly-Phe, was enh
anced up to 3-fold in the heat-adapted ribosomes. The adaptive enhance
ment was due to the large ribosomal subunit as demonstrated earlier by
heterologous recombination of ribosomal subunits, obtained from the p
lants pretreated by different temperatures. According to this, the pat
tern of ribosomal proteins of the large subunit exhibited pronounced d
ifferences as a function of preadaptation temperature: one spot increa
sed markedly in the protein staining intensity on the two-dimensional
polyacrylamide gels, while another almost disappeared. Two minor prote
in spots disappeared at high preadaptation temperatures. An evaluation
of the protein phosphorylation of ribosomal proteins yielded a decrea
sed P-32-label degree in case of the small subunit of heat-adapted rib
osomes. These results are considered to be an important molecular corr
elation to phenotypical temperature adaptation of in vivo protein synt
hesis in wheat, where the optimum temperature of C-14-leucine incorpor
ation into the total protein fraction, as a measure of in vivo protein
synthesis, shifts to higher grades with increasing preadaptation temp
erature of the wheat seedlings. Besides Triticum aestivum L. (spring w
heat; cv. Kolibri), heat adaptation potentials of T dicoccoides (tetra
ploid), T. longissimum (2n), T monococcum (2n), T. speltoides (2n) and
T tauschii (2n) were investigated. The temperature coefficient mu (ap
parent activation energy) also underwent adaptive alterations, althoug
h these changes were not unidirectional. T tauschii proved to be the s
pecies with the most pronounced adaptive potential in the high tempera
ture range, surpassed only by the heat adaptability of 14 d-postanthes
is caryopses: its optimum temperature of in vivo protein synthesis ros
e by more than 20-degrees-C after a 38-degrees-C-preadaptation period
(2 d).