Plant sphingolipid fatty acid 2-hydroxylases have unique characters unlike their animal and fungus counterparts

Plant Signal Behav. 2012 Nov;7(11):1388-92. doi: 10.4161/psb.21825. Epub 2012 Aug 23.

Abstract

2-Hydroxy fatty acids mainly contained in sphingolipids are synthesized by a sphingolipid fatty acid 2-hydroxylase (FAH). Recently, two FAH homologs in Arabidopsis thaliana (AtFAH1 and AtFAH2), without any cytochrome b₅(Cb5)-like domains, which are essential for the function of Saccharomyces cerevisiae and mammalian FAH, were identified and both AtFAHs were shown to be activated by the interaction with Cb5. In this study, we compared FAHs of various plants, animals and fungi. Interestingly, only plants had two FAH homologs and none of plant FAHs had any Cb5-like domains. In addition, we showed from the interaction and expression analyses that AtFAHs interacted with multiple Cb5s probably in various tissues. Thus, plant FAHs may have evolved unlike animal and fungus FAHs.

Keywords: cytochrome b5; interaction; sphingolipid fatty acid 2-hydroxylase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism*
  • Cytochromes b5 / genetics
  • Cytochromes b5 / metabolism
  • Mixed Function Oxygenases / genetics
  • Mixed Function Oxygenases / metabolism*
  • Protein Binding
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism

Substances

  • Arabidopsis Proteins
  • Saccharomyces cerevisiae Proteins
  • Cytochromes b5
  • Mixed Function Oxygenases
  • fatty acid 2-hydroxylase 1, Arabidopsis
  • fatty acid 2-hydroxylase 2, Arabidopsis