Trierixin, a novel Inhibitor of ER stress-induced XBP1 activation from Streptomyces sp. II. structure elucidation

J Antibiot (Tokyo). 2007 Sep;60(9):582-5. doi: 10.1038/ja.2007.74.

Abstract

Trierixin, a new member of the triene-ansamycin group, has been isolated from the fermentation broth of Streptomyces sp. AC654 as an inhibitor of ER stress-induced XBP1 activation. The structure of trierixin was determined on the basis of its spectroscopical and chemical properties. Trierixin possessed a 21-membered macrocyclic lactam, which contains a methylthio-benzenediol structure, and a cyclohexanecarbonylalanine moiety. Trierixin is thus elucidated as 21-thiomethylmycotrienin II.

MeSH terms

  • DNA-Binding Proteins / antagonists & inhibitors
  • Fermentation
  • HeLa Cells
  • Humans
  • Hydroquinones / chemistry
  • Hydroquinones / isolation & purification
  • Lactams, Macrocyclic / chemistry*
  • Lactams, Macrocyclic / isolation & purification
  • Magnetic Resonance Spectroscopy
  • Mass Spectrometry
  • Nuclear Proteins / antagonists & inhibitors
  • Optical Rotation
  • Regulatory Factor X Transcription Factors
  • Spectrophotometry, Ultraviolet
  • Streptomyces / chemistry*
  • Transcription Factors
  • Transition Temperature
  • X-Box Binding Protein 1

Substances

  • DNA-Binding Proteins
  • Hydroquinones
  • Lactams, Macrocyclic
  • Nuclear Proteins
  • Regulatory Factor X Transcription Factors
  • Transcription Factors
  • X-Box Binding Protein 1
  • XBP1 protein, human
  • trierixin
  • mycotrienin II