STRESS PROTEIN CSP 310 CAUSES OXIDATION AND PHOSPHORYLATION UNCOUPLING DURING LOW-TEMPERATURE STRESS ONLY IN CEREAL BUT NOT IN DYCOTYLEDON MITOCHONDRIA

Abstract

It was found that an addition of antiserum obtained against stress protein 310 kD increased coupling of oxidation and phosphorylation in mitochondria isolated from cold-stress winter rye shoots and had no influence on dycotiledon mitochondria (pumpkins and sunflower). The data obtained showed a difference between molecular weights of dycotyledon polypeptides with immunochemical affinity to CSP 310 and CSP 310 subunits. It was shown that low-temperature stress caused a transition to a low-energy state (“cold uncoupling”) of free from endogenous free fatty acid cereal mitochondria. At the same time, this “cold uncoupling” in mitochondria of dycotyledon species investigated was not detected. We suppose that a special mechanism of low-temperature stress reaction in mitochondria dealing with uncoupling activity of stress protein CSP 310 exists in cereals.

ACKNOWLEDGMENTS

This work was performed, in part, with the support of the Russian Foundation of Basic Research (project 00-04-48093).