Comparative Genomics of Trace Elements: Emerging Dynamic View of Trace Element Utilization and Function

Zhang, Yan; Gladyshev, Vadim N.

doi:10.1021/cr800557s

Cited by 120 publications

(109 citation statements)

References 510 publications

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“…Selenoproteins occur in some, but not all, organisms, e.g., in about half of eukaryotes and ϳ10% of archaea (384,385). This observation was utilized in a comparative analysis of completely sequenced genomes for Sec insertion machinery as proxy for Sec utilization and identification of additional components involved in Sec biosynthesis.…”

Section: B Seryl-trna Synthetasementioning

confidence: 99%

Selenoproteins: Molecular Pathways and Physiological Roles

Labunskyy

Hatfield

Gladyshev³

2014

Physiological Reviews

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1,024

835

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Selenium is an essential micronutrient with important functions in human health and relevance to several pathophysiological conditions. The biological effects of selenium are largely mediated by selenium-containing proteins (selenoproteins) that are present in all three domains of life. Although selenoproteins represent diverse molecular pathways and biological functions, all these proteins contain at least one selenocysteine (Sec), a seleniumcontaining amino acid, and most serve oxidoreductase functions. Sec is cotranslationally inserted into nascent polypeptide chains in response to the UGA codon, whose normal function is to terminate translation. To decode UGA as Sec, organisms evolved the Sec insertion machinery that allows incorporation of this amino acid at specific UGA codons in a process requiring a cis-acting Sec insertion sequence (SECIS) element. Although the basic mechanisms of Sec synthesis and insertion into proteins in both prokaryotes and eukaryotes have been studied in great detail, the identity and functions of many selenoproteins remain largely unknown. In the last decade, there has been significant progress in characterizing selenoproteins and selenoproteomes and understanding their physiological functions. We discuss current knowledge about how these unique proteins perform their functions at the molecular level and highlight new insights into the roles that selenoproteins play in human health.

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Section: B Seryl-trna Synthetasementioning

confidence: 99%

Selenoproteins: Molecular Pathways and Physiological Roles

Labunskyy

Hatfield

Gladyshev³

2014

Physiological Reviews

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1,024

835

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“…These three transition metals are also found in active centers of diverse proteins and act as electron acceptors and donors in numerous cellular processes, particularly in the chloroplast in the green lineage ( Fig. 1) (56,94). Among the different transition metals, Fe is the most widely utilized.…”

Section: The Use Of Metals In Plant Cell Biologymentioning

confidence: 99%

Copper and Iron Homeostasis in Plants: The Challenges of Oxidative Stress

Ravet

Pilon

2013

Antioxidants & Redox Signaling

204

162

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Significance: Photosynthesis, the process that drives life on earth, relies on transition metal (e.g., Fe and Cu) containing proteins that participate in electron transfer in the chloroplast. However, the light reactions also generate high levels of reactive oxygen species (ROS), which makes metal use in plants a challenge. Recent Advances: Sophisticated regulatory networks govern Fe and Cu homeostasis in response to metal ion availability according to cellular needs and priorities. Molecular remodeling in response to Fe or Cu limitation leads to its economy to benefit photosynthesis. Fe toxicity is prevented by ferritin, a chloroplastic Fe-storage protein in plants. Recent studies on ferritin function and regulation revealed the interplay between iron homeostasis and the redox balance in the chloroplast. Critical Issues: Although the connections between metal excess and ROS in the chloroplast are established at the molecular level, the mechanistic details and physiological significance remain to be defined. The causality/effect relationship between transition metals, redox signals, and responses is difficult to establish. Future Directions: Integrated approaches have led to a comprehensive understanding of Cu homeostasis in plants. However, the biological functions of several major families of Cu proteins remain unclear. The cellular priorities for Fe use under deficiency remain largely to be determined. A number of transcription factors that function to regulate Cu and Fe homeostasis under deficiency have been characterized, but we have not identified regulators that mediate responses to excess. Importantly, details of metal sensing mechanisms and cross talk to ROS-sensing mechanisms are so far poorly documented in plants. Antioxid. Redox Signal. 19,[919][920][921][922][923][924][925][926][927][928][929][930][931][932]

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“…Due to Gladyshev and his colleagues' identifying the selenoproteins in virtually all organisms whose genomes have been sequenced, it is known that 80% of prokaryotes lack the ability to incorporate selenium into protein as Sec, whereas 50% of eukaryotes utilize Sec (65). He extended these approaches to copper, molybdenum, cobalt, and nickel, providing insights into the biology of these elements (66).…”

Section: Areas Of Interest In Redox Biologymentioning

confidence: 99%

Redox Pioneer: Professor Vadim N. Gladyshev

Hatfield

2016

Antioxidants & Redox Signaling

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Professor Vadim N. Gladyshev is recognized here as a Redox Pioneer, because he has published an article on antioxidant/redox biology that has been cited more than 1000 times and 29 articles that have been cited more than 100 times. Gladyshev is world renowned for his characterization of the human selenoproteome encoded by 25 genes, identification of the majority of known selenoprotein genes in the three domains of life, and discoveries related to thiol oxidoreductases and mechanisms of redox control. Gladyshev's first faculty position was in the Department of Biochemistry, the University of Nebraska. There, he was a Charles Bessey Professor and Director of the Redox Biology Center. He then moved to the Department of Medicine at Brigham and Women's Hospital, Harvard Medical School, where he is Professor of Medicine and Director of the Center for Redox Medicine. His discoveries in redox biology relate to selenoenzymes, such as methionine sulfoxide reductases and thioredoxin reductases, and various thiol oxidoreductases. He is responsible for the genome-wide identification of catalytic redox-active cysteines and for advancing our understanding of the general use of cysteines by proteins. In addition, Gladyshev has characterized hydrogen peroxide metabolism and signaling and regulation of protein function by methionine-R-sulfoxidation. He has also made important contributions in the areas of aging and lifespan control and pioneered applications of comparative genomics in redox biology, selenium biology, and aging. Gladyshev's discoveries have had a profound impact on redox biology and the role of redox control in health and disease. He is a true Redox Pioneer. Antioxid. Redox Signal. 25, 1-9.

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Comparative Genomics of Trace Elements: Emerging Dynamic View of Trace Element Utilization and Function

Cited by 120 publications

References 510 publications

Selenoproteins: Molecular Pathways and Physiological Roles

Selenoproteins: Molecular Pathways and Physiological Roles

Copper and Iron Homeostasis in Plants: The Challenges of Oxidative Stress

Redox Pioneer: Professor Vadim N. Gladyshev

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