Pyruvate-sensitive AOX exists as a non-covalently associated dimer in the homeothermic spadix of the skunk cabbage, Symplocarpus renifolius

Yoshihiko Onda, Yoshiaki Kato, Yukie Abe, Takanori Ito, Yasuko Ito-Inaba, Miyuki Morohashi, Yuka Ito, Megumi Ichikawa, Kazushige Matsukawa, Minoru Otsuka, Hiroyuki Koiwa, Kikukatsu Ito

Research output: Contribution to journalArticlepeer-review

30 Citations (Scopus)

Abstract

The cyanide-resistant alternative oxidase (AOX) is a homodimeric protein whose activity can be regulated by the oxidation/reduction state and by α-keto acids. To further clarify the role of AOX in the skunk cabbage, Symplocarpus renifolius, we have performed expression and functional analyses of the encoding gene. Among the various tissues in the skunk cabbage, SrAOX transcripts were found to be specifically expressed in the thermogenic spadix. Moreover, our data demonstrate that the SrAOX protein exists as a non-covalently associated dimer in the thermogenic spadix, and is more sensitive to pyruvate than to other carboxylic acids. Our results suggest that the pyruvate-mediated modification of SrAOX activity plays a significant role in thermoregulation in the skunk cabbage.

Original languageEnglish
Pages (from-to)5852-5858
Number of pages7
JournalFEBS Letters
Volume581
Issue number30
DOIs
Publication statusPublished - 2007 Dec 22
Externally publishedYes

Keywords

  • Alternative oxidase
  • Mitochondria
  • Pyruvate
  • Respiration
  • Skunk cabbage
  • Thermogenic plants

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint

Dive into the research topics of 'Pyruvate-sensitive AOX exists as a non-covalently associated dimer in the homeothermic spadix of the skunk cabbage, Symplocarpus renifolius'. Together they form a unique fingerprint.

Cite this