Unraveling ferulate role in suberin and periderm biology by reverse genetics

Plant Signal Behav. 2010 Aug;5(8):953-8. doi: 10.4161/psb.5.8.12405. Epub 2010 Aug 1.

Abstract

Plant cell walls are dramatically affected by suberin deposition, becoming an impermeable barrier to water and pathogens. Suberin is a complex layered heteropolymer that comprises both a poly(aliphatic) and a poly(aromatic) lignin-like domain. Current structural models for suberin attribute the crosslinking of aliphatic and aromatic domains within the typical lamellar ultrastructure of the polymer to esterified ferulate. BAHD feruloyl transferases involved in suberin biosynthesis have been recently characterized in Arabidopsis and potato (Solanum tuberosum). In defective mutants, suberin, even lacks most of the esterified ferulate, but maintains the typical lamellar ultrastructure. However, suberized tissues display increased water permeability, in spite of exhibiting a similar lipid load to wild type. Therefore, the role of ferulate in suberin needs to be reconsidered. Moreover, silencing the feruloyl transferase in potato turns the typical smooth skin of cv. Desirée into a rough scabbed skin distinctive of Russet varieties and impairs the normal skin maturation that confers resistance to skinning. Concomitantly to these changes, the skin of silenced potatoes shows an altered profile of soluble phenolics with the emergence of conjugated polyamines.

Publication types

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

MeSH terms

  • Acyltransferases / genetics
  • Arabidopsis / enzymology
  • Arabidopsis / genetics
  • Cell Wall / chemistry
  • Cell Wall / ultrastructure*
  • Coumaric Acids / metabolism*
  • Gene Expression Regulation, Plant
  • Gene Silencing
  • Lipids / biosynthesis*
  • Plant Proteins / genetics
  • Polyamines / chemistry
  • Solanum tuberosum / enzymology
  • Solanum tuberosum / genetics
  • Water / physiology*

Substances

  • Coumaric Acids
  • Lipids
  • Plant Proteins
  • Polyamines
  • Water
  • suberin
  • ferulic acid
  • Acyltransferases