Adaptive Potential of Wheat Ribosomes toward Heat Depends on the Large Ribosomal Subunit and Ribosomal Protein Phosphorylation
Open Access
- 1 July 1988
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 87 (3), 562-565
- https://doi.org/10.1104/pp.87.3.562
Abstract
In a study of the translational efficiency of ribosomal subunits as a function of an in vivo temperature pretreatment, ribosomes were isolated from heat-pretreated (36°C) and reference (20°C) wheat seedlings (Triticum aestivum L.). The efficiency of recombined subunits in translating polyuridylic acid was assessed. A threefold increase in the rate of incorporation of phenylalanine by ribosomes from heat-pretreated plants was due to the large ribosomal subunit. This adaptive temperature effect was not correlated with a higher thermal stability of ribosomes or subunits from heat-pretreated seedlings, and two-dimensional gel electrophoresis failed to detect structural alterations of ribosomal proteins. Phosphorylation of ribosomal proteins in vitro showed no differences between ribosomes or subunits from heat-pretreated and reference plants. Incubation with [32P]orthophosphate in vivo led to twice the amount of phosphate in ribosomal proteins from heat-pretreated wheat seedlings. This result is important with respect to the evaluation of the molecular basis of enhanced translational efficiency of ribosomes isolated from heat-pretreated wheat seedlings.This publication has 22 references indexed in Scilit:
- PHOSPHORYLATION OF RIBOSOMAL-PROTEIN S6 BY CAMP-DEPENDENT PROTEIN-KINASE AND MITOGEN-STIMULATED S6 KINASE DIFFERENTIALLY ALTERS TRANSLATION OF GLOBIN MESSENGER-RNA1987
- The regulation of ribosomal protein S-6 phosphorylation in Xenopus oocytes: A potential role for intracellular pHDevelopmental Biology, 1984
- CHANGES IN RIBOSOME FUNCTION BY CAMP-DEPENDENT AND CAMP-INDEPENDENT PHOSPHORYLATION OF RIBOSOMAL PROTEIN-S61983
- Heat-shock-induced alterations of ribosomal protein phosphorylation in plant cell culturesCell, 1982
- The activity of the acidic phosphoproteins from the 80 S rat liver ribosome.Journal of Biological Chemistry, 1982
- Turnover Rates of Phosphoryl Groups in Ribosomal Proteins of Physarum polycephalumEuropean Journal of Biochemistry, 1981
- Mode of Degradation of Ribosomes in Regenerating Rat Liver in vivoEuropean Journal of Biochemistry, 1974
- Properties of hybrid ribosomes formed from the subunits of mesophilic and thermophilic bacteriaJournal of Molecular Biology, 1971
- Ribosomal proteins of Escherichia coli. I. Purification of the 30 S ribosomal proteinsBiochemistry, 1969
- Correlation of maximal growth temperature and ribosome heat stability.Proceedings of the National Academy of Sciences, 1967