The mitochondrial small heat-shock protein protects NADH:ubiquinone oxidoreductase of the electron transport chain during heat stress in plants

FEBS Lett. 1998 Jul 3;430(3):246-50. doi: 10.1016/s0014-5793(98)00669-3.

Abstract

Functional inactivation of the mitochondrial small heat-shock protein (lmw Hsp) in submitochondrial vesicles using protein-specific antibodies indicated that this protein protects NADH:ubiquinone oxidoreductase (complex I), and consequently electron transport from complex I to cytochrome c:O2 oxidoreductase (complex IV). Lmw Hsp function completely accounted for heat acclimation of complex I electron transport in pre-heat-stressed plants. Addition of purified lmw Hsp to submitochondrial vesicles lacking this Hsp increased complex I electron transport rates 100% in submitochondrial vesicles assayed at high temperatures. These results indicate that production of the mitochondrial lmw Hsp is an important adaptation to heat stress in plants.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Electron Transport / physiology
  • Fruit / metabolism*
  • Heat-Shock Proteins / isolation & purification
  • Heat-Shock Proteins / pharmacology
  • Heat-Shock Proteins / physiology*
  • Hot Temperature*
  • Mitochondria / metabolism
  • Multienzyme Complexes / metabolism
  • NAD(P)H Dehydrogenase (Quinone) / metabolism*
  • NADH, NADPH Oxidoreductases / metabolism
  • Oxidative Phosphorylation
  • Plant Proteins / isolation & purification
  • Plant Proteins / pharmacology
  • Plant Proteins / physiology*

Substances

  • Heat-Shock Proteins
  • LMW heat shock protein, Fragaria x ananassa
  • Multienzyme Complexes
  • Plant Proteins
  • NADH oxidase
  • NADH, NADPH Oxidoreductases
  • NAD(P)H Dehydrogenase (Quinone)