On the interaction site of serine acetyltransferase in the cysteine synthase complex from Escherichia coli

Chunhui Zhao, Yudai Moriga, Bin Feng, Yoichi Kumada, Hiroyuki Imanaka, Koreyoshi Imamura, Kazuhiro Nakanishi

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

Cysteine synthase from Escherichia coli is a bienzyme complex comprised of serine acetyltransferase (SAT) and O-acetylserine sulfhydrylase A. The site of interaction of a SAT molecule was investigated by gel chromatography and surface plasmon technique using various mutant-type SATs, to better understand the mechanism involved in complex formation. The C-terminus of SAT, Ile 273, along with Glu 268 and Asp 271, was found to be essential for complex formation. The effects of O-acetyl-l-serine and sulfide on the affinity for the complex formation were also studied using a surface plasmon technique.

Original languageEnglish
Pages (from-to)911-916
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume341
Issue number4
DOIs
Publication statusPublished - Mar 24 2006

Keywords

  • Cysteine synthase
  • O-Acetylserine sulfhydrylase
  • Protein-protein interaction
  • Serine acetyltransferase
  • Surface plasmon resonance

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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