Synthesis of the sulfur amino acids: cysteine and methionine

Wirtz, Markus; Droux, Michel

doi:10.1007/s11120-005-8810-9

Cited by 142 publications

(106 citation statements)

References 150 publications

(187 reference statements)

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“…Amino acid biosynthesis pathways are all closely tied to central metabolism, and frequently their products are an intrinsic part of this metabolism. For example, glutamate and glutamine are essential components in the GS-GOGAT system for nitrogen assimilation (Suzuki and Knaff 2005), serine and glycine are essential in single-carbon metabolism (Newman & Magasanik, 1963), cysteine and methionine are central to sulfur uptake and metabolism (Wirtz and Droux 2005); many amino acids are also involved in small molecule/cofactor synthesis (Fischer et al 2010;White, 2001) and even RNA modification (Grosjean and Benne 1998;Ikeuchi et al 2010;Suzuki and Miyauchi 2010). Therefore, we can reasonably separate the question of the functional chemical origin of many (if not most) amino acids from their incorporation in proteins via the semantics of a genetic code.…”

Section: Aminoacylation and The Genetic Codementioning

confidence: 99%

Molecular Evolution of Aminoacyl tRNA Synthetase Proteins in the Early History of Life

Fournier

Andam

Alm

et al. 2011

Orig Life Evol Biosph

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Aminoacyl-tRNA synthetases (aaRS) consist of several families of functionally conserved proteins essential for translation and protein synthesis. Like nearly all components of the translation machinery, most aaRS families are universally distributed across cellular life, being inherited from the time of the Last Universal Common Ancestor (LUCA). However, unlike the rest of the translation machinery, aaRS have undergone numerous ancient horizontal gene transfers, with several independent events detected between domains, and some possibly involving lineages diverging before the time of LUCA. These transfers reveal the complexity of molecular evolution at this early time, and the chimeric nature of genomes within cells that gave rise to the major domains. Additionally, given the role of these protein families in defining the amino acids used for protein synthesis, sequence reconstruction of their pre-LUCA ancestors can reveal the evolutionary processes at work in the origin of the genetic code. In particular, sequence reconstructions of the paralog ancestors of isoleucyl-and valyl-RS provide strong empirical evidence that at least for this divergence, the genetic code did not co-evolve with the aaRSs; rather, both amino acids were already part of the genetic code before their cognate aaRSs diverged from their common ancestor. The implications of this observation for the early evolution of RNA-directed protein biosynthesis are discussed.

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Section: Aminoacylation and The Genetic Codementioning

confidence: 99%

Molecular Evolution of Aminoacyl tRNA Synthetase Proteins in the Early History of Life

Fournier

Andam

Alm

et al. 2011

Orig Life Evol Biosph

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“…Although the final 10 amino acids are highly divergent between bacterial and plant SAT, the interaction is largely dependent on the C-terminal isoleucine in both cases (Campanini et al, 2005;Francois et al, 2006). Detailed comparisons of structure and reaction mechanism of Arabidopsis and bacterial SAT and OAS-TLs are available (Wirtz and Droux, 2005;Hell and Wirtz, 2008;Yi et al, 2010).…”

Section: Structure-function Relations Of the Cysteine Synthase Complexmentioning

confidence: 99%

Molecular Biology, Biochemistry and Cellular Physiology of Cysteine Metabolism inArabidopsis thaliana

Hell

Wirtz

2011

The Arabidopsis Book

Self Cite

109

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Cysteine is one of the most versatile molecules in biology, taking over such different functions as catalysis, structure, regulation and electron transport during evolution. Research on Arabidopsis has contributed decisively to the understanding of cysteine synthesis and its role in the assimilatory pathways of S, N and C in plants. The multimeric cysteine synthase complex is present in the cytosol, plastids and mitochondria and forms the centre of a unique metabolic sensing and signaling system. Its association is reversible, rendering the first enzyme of cysteine synthesis active and the second one inactive, and vice-versa. Complex formation is triggered by the reaction intermediates of cysteine synthesis in response to supply and demand and gives rise to regulation of genes of sulfur metabolism to adjust cellular sulfur homeostasis. Combinations of biochemistry, forward and reverse genetics, structural-and cell-biology approaches using Arabidopsis have revealed new enzyme functions and the unique pattern of spatial distribution of cysteine metabolism in plant cells. These findings place the synthesis of cysteine in the centre of the network of primary metabolism.

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“…An equally important aspect of Cys is that is the precursor molecule of an enormous number of sulfur-containing metabolites essential for the development of plant life. These metabolites include the other sulfur amino acid, methionine, vitamins such as biotin and thiamine, cofactors such as S-adenosylmethionine (SAM), coenzyme A, molybdenum cofactor (CoMo), and lipoic acid and iron-sulfur clusters that participate in the electron transport (Droux 2004 ;Wirtz and Droux 2005 ;Van Hoewyk et al 2008 ). Special mention deserves the antioxidant glutathione (GSH), regarded major determinant of cellular redox homeostasis (Foyer and Noctor 2011 ;Noctor et al 2012 ), which is based on the reactivity of its thiol group.…”

Section: Introductionmentioning

confidence: 99%

Signaling in the plant cytosol: cysteine or sulfide?

et al. 2014

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Cysteine (Cys) is the first organic compound containing reduced sulfur that is synthesized in the last stage of plant photosynthetic assimilation of sulfate. It is a very important metabolite not only because it is crucial for the structure, function and regulation of proteins but also because it is the precursor molecule of an enormous number of sulfur-containing metabolites essential for plant health and development. The biosynthesis of Cys is accomplished by the sequential reaction of serine acetyltransferase (SAT) and O-acetylserine(thiol)synthase (OASTL). In Arabidopsis thaliana, the analysis of specific mutants of members of the SAT and OASTL families has demonstrated that the cytosol is the compartment where the bulk of Cys synthesis takes place and that the cytosolic OASTL enzyme OAS-A1 is the responsible enzyme. Another member of the OASTL family is DES1, a novel L-cysteine desulfhydrase that catalyzes the desulfuration of Cys to produce sulfide, thus acting in a manner opposite to that of OAS-A1. Detailed studies of the oas-a1 and

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Synthesis of the sulfur amino acids: cysteine and methionine

Cited by 142 publications

References 150 publications

Molecular Evolution of Aminoacyl tRNA Synthetase Proteins in the Early History of Life

Molecular Evolution of Aminoacyl tRNA Synthetase Proteins in the Early History of Life

Molecular Biology, Biochemistry and Cellular Physiology of Cysteine Metabolism inArabidopsis thaliana

Signaling in the plant cytosol: cysteine or sulfide?

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