Post-translational modification of indoleamine 2,3-dioxygenase: N-terminal modification and nitration

Hidetsugu Fujigaki, Kanako Takahashi, Suwako Fujigaki, Junichi Masuda, Osamu Takikawa, Sanford P. Markey, Mitsuru Seishima, Kuniaki Saito

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2 Citations (Scopus)


Indoleamine 2,3-dioxygenase (IDO) induction can deplete l-Trp in target cells, and this effect is partially responsible for the antimicrobial, antiviral, and antiproliferative activities of several cytokines. Although a lot of studies have indicated the biological importance of IDO, the post-translational modification of IDO remains unknown. In this study, we analyzed IDO protein by liquid chromatography and tandem mass spectrometry (LC-MS/MS) to find post-translational modifications. LC-MS/MS analysis revealed that: (1) immunoprecipitated-IDO from a human monocyte cell line has been processed to cleave the N-terminal methionine, and the resulting N-terminal alanine is acetylated; (2) peroxynitrite, an NO-derived reactive species, which can modify proteins via formation of 3-nitrotyrosine, induced nitration and inactivation of recombinant IDO, specifically nitrating Tyr15, 345, and 353 residues. We successfully revealed these two types of post-translational modifications of IDO, and further findings of the post-translational modification may shed light on the mechanisms of IDO induction.

Original languageEnglish
Pages (from-to)41-45
Number of pages5
JournalInternational Congress Series
Publication statusPublished - 01-11-2007
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General Medicine


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