scholarly journals β-Cyanoalanine Synthase Is a Mitochondrial Cysteine Synthase-Like Protein in Spinach and Arabidopsis

2000 ◽  
Vol 123 (3) ◽  
pp. 1163-1172 ◽  
Author(s):  
Yves Hatzfeld ◽  
Akiko Maruyama ◽  
Ahlert Schmidt ◽  
Masaaki Noji ◽  
Kimiharu Ishizawa ◽  
...  
Keyword(s):  
Cysteine Synthase ◽  
Cyanoalanine Synthase

scholarly journals A molecular switch in sulfur metabolism to reduce arsenic and enrich selenium in rice grain

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Sheng-Kai Sun ◽  
Xuejie Xu ◽  
Zhong Tang ◽  
Zhu Tang ◽  
Xin-Yuan Huang ◽  
...  
Keyword(s):  
Grain Quality ◽  
Sulfur Metabolism ◽  
Physical Interaction ◽  
Rice Grain ◽  
Yield Losses ◽  
Serine Acetyltransferase ◽  
Cysteine Synthase ◽  
Arsenic Tolerance ◽  
Arsenic Accumulation ◽  
Low Levels

AbstractRice grains typically contain high levels of toxic arsenic but low levels of the essential micronutrient selenium. Anthropogenic arsenic contamination of paddy soils exacerbates arsenic toxicity in rice crops resulting in substantial yield losses. Here, we report the identification of the gain-of-function arsenite tolerant 1 (astol1) mutant of rice that benefits from enhanced sulfur and selenium assimilation, arsenic tolerance, and decreased arsenic accumulation in grains. The astol1 mutation promotes the physical interaction of the chloroplast-localized O-acetylserine (thiol) lyase protein with its interaction partner serine-acetyltransferase in the cysteine synthase complex. Activation of the serine-acetyltransferase in this complex promotes the uptake of sulfate and selenium and enhances the production of cysteine, glutathione, and phytochelatins, resulting in increased tolerance and decreased translocation of arsenic to grains. Our findings uncover the pivotal sensing-function of the cysteine synthase complex in plastids for optimizing stress resilience and grain quality by regulating a fundamental macronutrient assimilation pathway.

Transgenic tobacco plants expressing a rice cysteine synthase gene are tolerant to toxic levels of cadmium

2001 ◽  
Vol 158 (5) ◽  
pp. 655-661 ◽  
Author(s):  
Emiko Harada ◽  
Yong-Eui Choi ◽  
Atsunari Tsuchisaka ◽  
Hitoshi Obata ◽  
Hiroshi Sano
Keyword(s):  
Transgenic Tobacco ◽  
Transgenic Tobacco Plants ◽  
Cysteine Synthase ◽  
Tobacco Plants

Cysteine synthase A overexpression inCorynebacterium glutamicumenhancesl-isoleucine production

2018 ◽  
Vol 66 (1) ◽  
pp. 74-81 ◽  
Author(s):  
Wenjian Ma ◽  
Jianli Wang ◽  
Ye Li ◽  
Xiaoyuan Wang
Keyword(s):  
Cysteine Synthase

Overexpression of a plant cysteine synthase gene and biosynthesis of a plant specific metabolite, β-(pyrazol-1-yl)-L-alanine, in Escherichia coli

1994 ◽  
Vol 72 (1) ◽  
pp. 188-192 ◽  
Author(s):  
Kazuki Saito ◽  
Reiko Kanda ◽  
Makoto Kurosawa ◽  
Isamu Murakoshi
Keyword(s):  
Escherichia Coli ◽  
Transcriptional Control ◽  
Spinacia Oleracea ◽  
Higher Plants ◽  
Total Soluble Protein ◽  
T7 Promoter ◽  
Cysteine Synthase ◽  
Mechanistic Investigation

Cysteine synthase (EC 4.2.99.8) in higher plants is responsible for biosynthesis of not only cysteine but also some nonprotein amino acids such as β-(pyrazol-1-yl)-L-alanine. The cDNA of a cysteine synthase from spinach (Spinacia oleracea) was inserted into pET8c (=pET3d) under the transcriptional control of strong T7 promoter to yield an overexpression vector pCEK1. The amount of the exogenous cysteine synthase was increased up to 40% of the total soluble protein of Escherichia coli transformed with pCEK1. β-(Pyrazol-1-yl)-L-alanine, a specific metabolite in plants of the Cucurbitaceae, was biosynthesized by overexpressed cysteine synthase from pyrazole in the presence of O-acetyl-L-serine and serine, in vitro and in vivo, respectively. The present study provides the system for mechanistic investigation of biosynthesis of cysteine and biogenetically related β-substituted alanines at molecular genetic level.

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