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

doi:10.1016/j.bbrc.2006.01.054

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 journal › Article › peer-review

43 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 language	English
Pages (from-to)	911-916
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	341
Issue number	4
DOIs	https://doi.org/10.1016/j.bbrc.2006.01.054
Publication status	Published - 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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10.1016/j.bbrc.2006.01.054

Cite this

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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.",

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AU - Zhao, Chunhui

AU - Moriga, Yudai

AU - Feng, Bin

AU - Kumada, Yoichi

AU - Imanaka, Hiroyuki

AU - Imamura, Koreyoshi

AU - Nakanishi, Kazuhiro

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AB - 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.

KW - Cysteine synthase

KW - O-Acetylserine sulfhydrylase

KW - Protein-protein interaction

KW - Serine acetyltransferase

KW - Surface plasmon resonance

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

Abstract

Keywords

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