Secondary structure of GPI attachment signal region monitored by circular dichroism

Yuri Ikeda, Daiki Takahashi, Keiya Inoue, Hiromu Sugita, Tatsuki Kikegawa, Kenji Etchuya

Research output: Contribution to journalArticle

Abstract

Secondary structure of the glycosylphosphatidylinositol attachment signal (GPI-AS) in GPI-anchored proteins, usually cleaved from the mature protein in eukaryotic cells, was evaluated using circular dichroism (CD). GPI-AS was expressed in Escherichia coli and was purified as a green fluorescent protein (GFP)-fused recombinant protein. The secondary structure was monitored by observing the far-UV CD bands. The α-helix content increased by 3.7% (indicates 13 amino acids) in GFP-fused GPI-AS, indicating that GPI-AS tends to have an α-helical structure. The method we propose in this study can be used to evaluate the secondary structure of the signal regions, which are absent in the mammalian mature proteins.

Original languageEnglish
Pages (from-to)1153-1155
Number of pages3
JournalChemistry Letters
Volume45
Issue number10
DOIs
Publication statusPublished - 1 Jan 2016

Keywords

  • Glycosylphosphatidylinositol attachment signal (GPI-AS)
  • Protein
  • Secondary structure

Cite this

Ikeda, Y., Takahashi, D., Inoue, K., Sugita, H., Kikegawa, T., & Etchuya, K. (2016). Secondary structure of GPI attachment signal region monitored by circular dichroism. Chemistry Letters, 45(10), 1153-1155. https://doi.org/10.1246/cl.160551