title: Influence of CSP 310 and CSP 310-like proteins from cereals on mitochondrial energetic activity and lipid peroxidation in vitro and in vivo.
abstract: BACKGROUND
  The development of chilling and freezing injury symptoms in plants is known to frequently coincide with peroxidation of free fatty acids. Mitochondria are one of the major sources of reactive oxygen species during cold stress. Recently it has been suggested that uncoupling of oxidation and phosphorylation in mitochondria during oxidative stress can decrease ROS formation by mitochondrial respiratory chain generation. At the same time, it is known that plant uncoupling mitochondrial protein (PUMP) and other UCP-like proteins are not the only uncoupling system in plant mitochondria. All plants have cyanide-resistant oxidase (AOX) whose activation causes an uncoupling of respiration and oxidative phosphorylation. Recently it has been found that in cereals, cold stress protein CSP 310 exists, and that this causes uncoupling of oxidation and phosphorylation in mitochondria.
  
  
  RESULTS
  We studied the effects of CSP 310-like native cytoplasmic proteins from a number of cereal species (winter rye, winter wheat, Elymus and maize) on the energetic activity of winter wheat mitochondria. This showed that only CSP 310 (cold shock protein with molecular weight 310 kD) caused a significant increase of non-phosphorylative respiration. CSP 310-like proteins of other cereals studied did not have any significant influence on mitochondrial energetic activity. It was found that among CSP 310-like proteins only CSP 310 had prooxidant activity. At the same time, Elymus CSP 310-like proteins have antioxidant activity. The study of an influence of infiltration by different plant uncoupling system activators (pyruvate, which activates AOX, and linoleic acid which is a substrate and activator for PUMP and CSP 310) showed that all of these decreased lipid peroxidation during cold stress.
  
  
  CONCLUSIONS
  Different influence of CSP 310-like proteins on mitochondrial energetic activity and lipid peroxidation presumably depend on the various subunit combinations in their composition. All the plant cell systems that caused an uncoupling of oxidation and phosphorylation in plant mitochondria can participate in plant defence from oxidative damage during cold stress.
authors.affiliation: Siberian Institute of Plant Physiology and Biochemistry, Russian Academy of Sciences, Irkutsk, Russia. akol@sifibr.irk.ru
authors.forename: A V
authors.initials: AV
authors.lastname: Kolesnichenko
authors.forename: V V
authors.initials: VV
authors.lastname: Zykova
authors.forename: O I
authors.initials: OI
authors.lastname: Grabelnych
authors.forename: N A
authors.initials: NA
authors.lastname: Koroleva
authors.forename: T P
authors.initials: TP
authors.lastname: Pobezhimova
authors.forename: Y M
authors.initials: YM
authors.lastname: Konstantinov
authors.forename: V K
authors.initials: VK
authors.lastname: Voinikov
mesh_terms: D002352:Carrier Proteins / Q000494:pharmacology*; D003080:Cold Temperature; D002523:Edible Grain / Q000737:chemistry*; D007473:Ion Channels; D019787:Linoleic Acid / Q000494:pharmacology; D015227:Lipid Peroxidation / Q000187:drug effects*; D008565:Membrane Proteins / Q000494:pharmacology*; D008928:Mitochondria / Q000187:drug effects* / Q000378:metabolism; D024101:Mitochondrial Proteins; D010085:Oxidative Phosphorylation / Q000187:drug effects; D010101:Oxygen Consumption / Q000187:drug effects; D010940:Plant Proteins / Q000494:pharmacology*; D018520:Plant Shoots / Q000187:drug effects / Q000378:metabolism; D019289:Pyruvic Acid / Q000494:pharmacology; D014908:Triticum / Q000187:drug effects / Q000378:metabolism; D000071256:Uncoupling Protein 1
chemical_list: D002352:Carrier Proteins; D007473:Ion Channels; D008565:Membrane Proteins; D024101:Mitochondrial Proteins; D010940:Plant Proteins; D000071256:Uncoupling Protein 1; D019289:Pyruvic Acid; D019787:Linoleic Acid