Heterogeneity of mitochondrial protein biogenesis during primary leaf development in barley

P Thompson, CG Bowsher, Alyson Kim Tobin

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)

Abstract

The natural developmental gradient of light-grown primary leaves of barley (Hordeum vulgare L..) was used to analyze the biogenesis of mitochondrial proteins in relation to the age and physiological changes within the leaf. The data indicate that the protein composition of mitochondria changes markedly during leaf development. Three distinct patterns of protein development were noted: group A proteins, consisting of the E1 beta-subunit of the pyruvate dehydrogenase complex, ORF156, ORF577, alternative oxidase, RPS12, cytochrome oxidase subunits II and III, malic enzyme, and the alpha- and beta-subunits of F-1-ATPase; group B proteins, consisting of the E1 alpha-subunit of the pyruvate dehydrogenase complex, isocitrate dehydrogenase, HSP70A, cpn60C, and cpn60B; and group C proteins, consisting of the four subunits of the glycine decarhoxylase complex (P, H, T, and L proteins), fumarase, and formate dehydrogenase. All of the proteins increased in concentration from the basal meristem to the end of the elongation zone (20.0 mm from the leaf base), whereupon group A proteins decreased, group B proteins increased to a maximum at 50 mm from the leaf base, and group C proteins increased to a maximum at the leaf tip. This study provides evidence of a marked heterogeneity of mitochondrial protein composition, reflecting a changing function as leaf cells develop photosynthetic and photorespiratory capacity.

Original languageEnglish
Pages (from-to)1089-1099
Number of pages11
JournalPlant Physiology
Volume118
Issue number3
DOIs
Publication statusPublished - Nov 1998

Keywords

  • TRITICUM-AESTIVUM-L
  • PYRUVATE-DEHYDROGENASE COMPLEX
  • CELL-SPECIFIC DISTRIBUTION
  • HIGHER-PLANT MITOCHONDRIA
  • CYTOCHROME-C-OXIDASE
  • NAD MALIC ENZYME
  • PISUM-SATIVUM-L
  • GLYCINE DECARBOXYLASE
  • ALTERNATIVE OXIDASE
  • MONOCLONAL-ANTIBODIES

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