Regulation of ethylene levels in canola (Brassica campestris) by 1-aminocyclopropane-1-carboxylate deaminase-containing Methylobacterium fujisawaense

Planta. 2006 Jul;224(2):268-78. doi: 10.1007/s00425-005-0211-y. Epub 2006 Jan 17.

Abstract

We report the presence of ACC deaminase in Methylobacterium fujisawaense and its lowering of ethylene levels and promotion of root elongation in canola seedlings under gnotobiotic conditions. To test a part of the previous model proposed for ACC deaminase producing bacteria with Methylobacterium, ACC levels and various enzyme activities were monitored in canola. Lower amounts of ACC were present in the tissues of seeds treated with M. fujisawaense strains than in control seeds treated with MgSO(4). Though the increased activities of ACC synthase in the tissue extracts of the treated seedlings might be due to bacterial indole-3-acetic acid, the amount of ACC was reduced due to bacterial ACC deaminase activity. The activities of ACC oxidase, the enzyme catalyzing conversion of ACC to ethylene remained lower in M. fujisawaense treated seedlings. This consequently lowered the ethylene in plants and prevented ethylene inhibition of root elongation. Our results collectively suggest that Methylobacterium commonly found in soils, as well as on the surfaces of leaves, seeds, and in the rhizosphere of a wide variety of plants could be better exploited to promote plant growth.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Brassica / growth & development
  • Brassica / metabolism*
  • Brassica / microbiology*
  • Carbon-Carbon Lyases / metabolism*
  • Cytokinins / metabolism
  • Ethylenes / biosynthesis
  • Ethylenes / metabolism*
  • Indoleacetic Acids / metabolism
  • Methylobacterium / enzymology*
  • Models, Biological
  • Plant Roots / enzymology
  • Plant Roots / growth & development
  • Seedlings / microbiology

Substances

  • Cytokinins
  • Ethylenes
  • Indoleacetic Acids
  • indoleacetic acid
  • ethylene
  • 1-aminocyclopropane-1-carboxylate deaminase
  • Carbon-Carbon Lyases