Selenocysteine in Proteins—Properties and Biotechnological Use
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The Selenium Recycling Enzyme Selenocysteine Lyase: Regulation and Physiological Role in Glucose and Lipid Metabolism
THE SELENIUM RECYCLING ENZYME SELENOCYSTEINE LYASE: REGULATION AND PHYSIOLOGICAL ROLE IN GLUCOSE AND LIPID METABOLISM A DISSERTATION SUBMITTED TO THE GRADUATE DIVISION OF THE UNIVERSITY OF HAWAI‘I AT MĀNOA IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE OF DOCTOR OF PHILOSOPHY IN CELL AND MOLECULAR BIOLOGY MAY 2012 BY LUCIA ANDREIA SEALE Dissertation Committee: Marla J. Berry, Chairperson Robert A. Nichols Jun Pane‘e P. Reed Larsen E. Gordon Grau To my beloved parents Wilson & Madalena To my dear love André ii ACKNOWLEDGEMENTS A Ph.D. is a journey in a rough sea. As in all memorable expeditions, there is more to learn while traveling towards the final destination than at the destination itself. In several ways, it is the path and how you face the unexpected obstacles in this path that makes you a Doctor. The Ph.D. expedition does not allow an easy ride. While you travel through the waves and storms of your topic, figuring out a lot on and about yourself, you also encounter along the way people that make your stressful journey happier, nicer, safer, funnier and – why not – more challenging. They provided the emotional background that is not described in a scientific document. In my Ph.D. journey, these are the people about whom I’ll talk years ahead to friends, to whom I will silently smile when the nostalgic waves of the Ph.D. path break in the shores of my life. They are the unforgettable people that allowed me to arrive safe and sound in Doctorland. First and foremost, my greatest acknowledgement and gratitude goes to Dr. -
Selenocysteine, Pyrrolysine, and the Unique Energy Metabolism of Methanogenic Archaea
Hindawi Publishing Corporation Archaea Volume 2010, Article ID 453642, 14 pages doi:10.1155/2010/453642 Review Article Selenocysteine, Pyrrolysine, and the Unique Energy Metabolism of Methanogenic Archaea Michael Rother1 and Joseph A. Krzycki2 1 Institut fur¨ Molekulare Biowissenschaften, Molekulare Mikrobiologie & Bioenergetik, Johann Wolfgang Goethe-Universitat,¨ Max-von-Laue-Str. 9, 60438 Frankfurt am Main, Germany 2 Department of Microbiology, The Ohio State University, 376 Biological Sciences Building 484 West 12th Avenue Columbus, OH 43210-1292, USA Correspondence should be addressed to Michael Rother, [email protected] andJosephA.Krzycki,[email protected] Received 15 June 2010; Accepted 13 July 2010 Academic Editor: Jerry Eichler Copyright © 2010 M. Rother and J. A. Krzycki. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Methanogenic archaea are a group of strictly anaerobic microorganisms characterized by their strict dependence on the process of methanogenesis for energy conservation. Among the archaea, they are also the only known group synthesizing proteins containing selenocysteine or pyrrolysine. All but one of the known archaeal pyrrolysine-containing and all but two of the confirmed archaeal selenocysteine-containing protein are involved in methanogenesis. Synthesis of these proteins proceeds through suppression of translational stop codons but otherwise the two systems are fundamentally different. This paper highlights these differences and summarizes the recent developments in selenocysteine- and pyrrolysine-related research on archaea and aims to put this knowledge into the context of their unique energy metabolism. 1. Introduction found to correspond to pyrrolysine in the crystal structure [9, 10] and have its own tRNA [11]. -
Selenocysteine, Identified As the Penultimate C-Terminal Residue in Human T-Cell Thioredoxin Reductase, Corresponds to TGA in the Human Placental Gene" (1996)
University of Nebraska - Lincoln DigitalCommons@University of Nebraska - Lincoln Vadim Gladyshev Publications Biochemistry, Department of June 1996 Selenocysteine, identified as the penultimate C-terminal esiduer in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene Vadim Gladyshev University of Nebraska-Lincoln, [email protected] Kuan-Teh Jeang National Institutes of Health, Bethesda, MD Thressa C. Stadtman National Institutes of Health, Bethesda, MD Follow this and additional works at: https://digitalcommons.unl.edu/biochemgladyshev Part of the Biochemistry, Biophysics, and Structural Biology Commons Gladyshev, Vadim; Jeang, Kuan-Teh; and Stadtman, Thressa C., "Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene" (1996). Vadim Gladyshev Publications. 23. https://digitalcommons.unl.edu/biochemgladyshev/23 This Article is brought to you for free and open access by the Biochemistry, Department of at DigitalCommons@University of Nebraska - Lincoln. It has been accepted for inclusion in Vadim Gladyshev Publications by an authorized administrator of DigitalCommons@University of Nebraska - Lincoln. Proc. Natl. Acad. Sci. USA Vol. 93, 6146-6151, June 1996 Biochemistrypp. Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene (selenium/thioredoxin reductase/TGA/selenocysteine) VADIM N. GLADYSHEV*, KUAN-TEH JEANGt, AND THRESSA C. STADTMAN*t *Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, and tLaboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 9000 Rockville Pike, Bethesda, MD 20892 Contributed by Thressa C. Stadtman, February 27, 1996 ABSTRACT The possible relationship of selenium to im- peroxidase family (8). -
Characterization of a Selenocysteine-Ligated P450 Compound I Reveals Direct Link Between Electron Donation and Reactivity Elizab
Characterization of a Selenocysteine-ligated P450 Compound I Reveals Direct Link Between Electron Donation and Reactivity Elizabeth Onderko†, Alexey Silakov†, Timothy H. Yosca‡, and Michael T. Green‡,* ‡Departments of Chemistry & Molecular Biology and Biochemistry, University of California, Irvine, CA 92697 †Department of Chemistry, Penn State University, University Park, PA 16802 Contact: [email protected] Abstract Strong electron-donation from the axial thiolate-ligand of cytochrome P450 has been proposed to increase the reactivity of compound I with respect to C–H bond activation. However, it has proven difficult to test this hypothesis, and a direct link between reactivity and electron donation has yet to be established. To make this connection, we have prepared a selenolate-ligated cytochrome P450 compound I intermediate. This isoelectronic perturbation allows for direct comparisons with the wild type enzyme. Selenium incorporation was obtained using a cysteine auxotrophic E. coli strain. The intermediate was prepared with meta-chloroperbenzoic acid and characterized by UV-visible, Mössbauer, and electron paramagnetic resonance spectroscopies. Measurements revealed increased asymmetry around the ferryl moiety, consistent with increased electron donation from the axial selenolate-ligand. In line with this observation, we find that the selenolate-ligated compound I cleaves C–H bonds more rapidly than the wild-type intermediate. Background Cytochrome P450s are a class of thiolate-ligated heme proteins that are known for their ability to functionalize unactivated C–H bonds. In efforts to understand reactivity in these and other thiolate-heme systems, comparisons are often drawn between P450s and the histidine-ligated heme peroxidases. Both classes of heme enzymes share a similar active intermediate: a ferryl (or iron(IV)oxo) radical species, called compound I1-3. -
Generation of Recombinant Mammalian Selenoproteins Through Ge- Netic Code Expansion with Photocaged Selenocysteine
bioRxiv preprint doi: https://doi.org/10.1101/759662; this version posted September 5, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Generation of Recombinant Mammalian Selenoproteins through Ge- netic Code Expansion with Photocaged Selenocysteine. Jennifer C. Peeler, Rachel E. Kelemen, Masahiro Abo, Laura C. Edinger, Jingjia Chen, Abhishek Chat- terjee*, Eranthie Weerapana* Department of Chemistry, Boston College, Chestnut Hill, Massachusetts 02467, United States Supporting Information Placeholder ABSTRACT: Selenoproteins contain the amino acid sele- neurons susceptible to ferroptotic cell death due to nocysteine and are found in all domains of life. The func- overoxidation and inactivation of GPX4-Cys.4 This ob- tions of many selenoproteins are poorly understood, servation demonstrates a potential advantage conferred partly due to difficulties in producing recombinant sele- by the energetically expensive production of selenopro- noproteins for cell-biological evaluation. Endogenous teins. mammalian selenoproteins are produced through a non- Sec incorporation deviates from canonical protein canonical translation mechanism requiring suppression of translation, requiring suppression of the UGA stop codon. the UGA stop codon, and a selenocysteine insertion se- In eukaryotes, Sec biosynthesis occurs directly on the quence (SECIS) element in the 3’ untranslated region of suppressor tRNA (tRNA[Ser]Sec). Specifically, tRNA[Ser]Sec the mRNA. Here, recombinant selenoproteins are gener- is aminoacylated with serine by seryl-tRNA synthetase ated in mammalian cells through genetic code expansion, (SerS), followed by phosphorylation by phosphoseryl- circumventing the requirement for the SECIS element, tRNA kinase (PSTK), and subsequent Se incorporation and selenium availability. -
Site-Specific Protein Modifications Through Pyrroline-Carboxy-Lysine Residues
Site-specific protein modifications through pyrroline-carboxy-lysine residues Weijia Ou1, Tetsuo Uno1, Hsien-Po Chiu, Jan Grünewald, Susan E. Cellitti, Tiffany Crossgrove, Xueshi Hao, Qian Fan, Lisa L. Quinn, Paula Patterson, Linda Okach, David H. Jones, Scott A. Lesley, Ansgar Brock, and Bernhard H. Geierstanger2 Genomics Institute of the Novartis Research Foundation, 10675 John-Jay-Hopkins Drive, San Diego, CA 92121-1125 Edited* by Peter G. Schultz, The Scripps Research Institute, La Jolla, CA, and approved May 11, 2011 (received for review April 4, 2011) Pyrroline-carboxy-lysine (Pcl) is a demethylated form of pyrrolysine acids will face similar hurdles to achieve site-specificity without that is generated by the pyrrolysine biosynthetic enzymes when deleterious effects to the protein of interest. the growth media is supplemented with D-ornithine. Pcl is readily The most elegant way to generate homogenously, site-specifi- incorporated by the unmodified pyrrolysyl-tRNA/tRNA synthetase cally modified proteins is the in vivo incorporation of unnatural pair into proteins expressed in Escherichia coli and in mammalian amino acids (7–9). Over 70 unnatural amino acids featuring a cells. Here, we describe a broadly applicable conjugation chemistry wide array of functionalities can be incorporated at TAG codons that is specific for Pcl and orthogonal to all other reactive groups using specific tRNA/tRNA synthetase pairs engineered through on proteins. The reaction of Pcl with 2-amino-benzaldehyde or an in vivo selection process to be orthogonal to the cellular 2-amino-acetophenone reagents proceeds to near completion at machinery of the host cells. A set of reactive unnatural amino neutral pH with high efficiency. -
Selenium Vs. Sulfur: Investigating the Substrate Specificity of a Selenocysteine Lyase
University of Central Florida STARS Electronic Theses and Dissertations, 2004-2019 2019 Selenium vs. Sulfur: Investigating the Substrate Specificity of a Selenocysteine Lyase Michael Johnstone University of Central Florida Part of the Biotechnology Commons Find similar works at: https://stars.library.ucf.edu/etd University of Central Florida Libraries http://library.ucf.edu This Masters Thesis (Open Access) is brought to you for free and open access by STARS. It has been accepted for inclusion in Electronic Theses and Dissertations, 2004-2019 by an authorized administrator of STARS. For more information, please contact [email protected]. STARS Citation Johnstone, Michael, "Selenium vs. Sulfur: Investigating the Substrate Specificity of a Selenocysteine Lyase" (2019). Electronic Theses and Dissertations, 2004-2019. 6511. https://stars.library.ucf.edu/etd/6511 SELENIUM VS. SULFUR: INVESTIGATING THE SUBSTRATE SPECIFICITY OF A SELENOCYSTEINE LYASE by MICHAEL ALAN JOHNSTONE B.S. University of Central Florida, 2017 A thesis submitted in partial fulfillment of the requirements for the degree of Master of Science in the Burnett School of Biomedical Sciences in the College of Medicine at the University of Central Florida Orlando, Florida Summer Term 2019 Major Professor: William T. Self © 2019 Michael Alan Johnstone ii ABSTRACT Selenium is a vital micronutrient in many organisms. While traces are required for survival, excess amounts are toxic; thus, selenium can be regarded as a biological “double-edged sword”. Selenium is chemically similar to the essential element sulfur, but curiously, evolution has selected the former over the latter for a subset of oxidoreductases. Enzymes involved in sulfur metabolism are less discriminate in terms of preventing selenium incorporation; however, its specific incorporation into selenoproteins reveals a highly discriminate process that is not completely understood. -
Virtual 2-D Map of the Fungal Proteome
www.nature.com/scientificreports OPEN Virtual 2‑D map of the fungal proteome Tapan Kumar Mohanta1,6*, Awdhesh Kumar Mishra2,6, Adil Khan1, Abeer Hashem3,4, Elsayed Fathi Abd‑Allah5 & Ahmed Al‑Harrasi1* The molecular weight and isoelectric point (pI) of the proteins plays important role in the cell. Depending upon the shape, size, and charge, protein provides its functional role in diferent parts of the cell. Therefore, understanding to the knowledge of their molecular weight and charges is (pI) is very important. Therefore, we conducted a proteome‑wide analysis of protein sequences of 689 fungal species (7.15 million protein sequences) and construct a virtual 2‑D map of the fungal proteome. The analysis of the constructed map revealed the presence of a bimodal distribution of fungal proteomes. The molecular mass of individual fungal proteins ranged from 0.202 to 2546.166 kDa and the predicted isoelectric point (pI) ranged from 1.85 to 13.759 while average molecular weight of fungal proteome was 50.98 kDa. A non‑ribosomal peptide synthase (RFU80400.1) found in Trichoderma arundinaceum was identifed as the largest protein in the fungal kingdom. The collective fungal proteome is dominated by the presence of acidic rather than basic pI proteins and Leu is the most abundant amino acid while Cys is the least abundant amino acid. Aspergillus ustus encodes the highest percentage (76.62%) of acidic pI proteins while Nosema ceranae was found to encode the highest percentage (66.15%) of basic pI proteins. Selenocysteine and pyrrolysine amino acids were not found in any of the analysed fungal proteomes. -
Rare, but Essential – the Amino Acid Selenocysteine
Molecular Biology Rare, but essential – the amino acid selenocysteine Based at the University of Bonn, Germany, Professor Dr Ulrich Schweizer is leading research into revealing the role of selenoproteins in mammalian physiology. By elucidating the mechanisms underlying their function, his work is yielding new insights into a wide array of human diseases affecting the brain and thyroid hormones. At the core of Prof Dr Schweizer’s research is the rare selenium-containing 21st amino acid selenocysteine (Sec), the defining component of selenoproteins. elenocysteine (Sec) is an the trace element selenium (Se) replaces the essential amino acid component sulphur atom of cysteine. Selenium possesses in selenoproteins, which are similar but more reactive properties than involved in a variety of cellular and sulphur, and is always housed in the active metabolic processes. Increasingly, centre of selenoenzymes. Stheir deregulation is being associated with neurodegenerative and other diseases, INVESTIGATING THE RAREST AMINO for which the underlying mechanisms ACID have remained unclear. However, using Sec eluded the Nobel Prize winning scientists novel transgenic mouse models, Prof Dr who deciphered the genetic code, because Schweizer and his team have uncovered Sec is encoded by what has been regarded a wealth of information regarding the exclusively as a termination codon, UGA. mechanisms behind their function. His team’s How can the cell distinguish between extensive research has found that reducing termination and Sec incorporation? There is a the expression of selenoproteins in the specific element within the mRNA sequence mammalian brain impairs brain development that directs the re-coding of UGA, called the and healthy functioning, consequently selenocysteine insertion sequence (SECIS). -
Purification and Characterization of a Novel Selenocysteine Lyase from Enterococcus Faecalis
University of Central Florida STARS Electronic Theses and Dissertations, 2004-2019 2014 Purification and Characterization of a Novel Selenocysteine Lyase from Enterococcus faecalis Samantha Nelson University of Central Florida Part of the Biotechnology Commons, and the Molecular Biology Commons Find similar works at: https://stars.library.ucf.edu/etd University of Central Florida Libraries http://library.ucf.edu This Masters Thesis (Open Access) is brought to you for free and open access by STARS. It has been accepted for inclusion in Electronic Theses and Dissertations, 2004-2019 by an authorized administrator of STARS. For more information, please contact [email protected]. STARS Citation Nelson, Samantha, "Purification and Characterization of a Novel Selenocysteine Lyase from Enterococcus faecalis" (2014). Electronic Theses and Dissertations, 2004-2019. 4807. https://stars.library.ucf.edu/etd/4807 PURIFICATION AND CHARACTERIZATION OF A NOVEL SELENOCYSTEINE LYASE FROM ENTEROCOCCUS FAECALIS by SAMANTHA NELSON B.S. University of Central Florida, 2012 A thesis submitted in partial fulfillment of the requirements for the degree of Master of Science in the Burnett School of Biomedical Sciences in the College of Medicine at the University of Central Florida Orlando, Florida Summer Term 2014 Major Professor: William T. Self © 2014 Samantha Nelson ii ABSTRACT A previous study identified Enterococcus faecalis as one of two bacteria known to have the selD gene and other selenium related genes without having the genes necessary to make selenocysteine or selenouridine. EF2570, a gene in the cluster, was later shown to be upregulated during biofilm formation and also responsible for a selenite- and molybdate-dependent increase in biofilm formation in vitro. -
Parental Selenium Nutrition Affects the One-Carbon Metabolism
life Article Parental Selenium Nutrition Affects the One-Carbon Metabolism and the Hepatic DNA Methylation Pattern of Rainbow Trout (Oncorhynchus mykiss) in the Progeny 1, 2, 1 1 Pauline Wischhusen y , Takaya Saito y ,Cécile Heraud , Sadasivam J. Kaushik , 1 2 1, , Benoit Fauconneau , Philip Antony Jesu Prabhu , Stéphanie Fontagné-Dicharry * y 2, and Kaja H. Skjærven y 1 INRAE, University of Pau and Pays de l’Adour, E2S UPPA, NUMEA, 64310 Saint Pee sur Nivelle, France; [email protected] (P.W.); [email protected] (C.H.); [email protected] (S.J.K.); [email protected] (B.F.) 2 Institute of Marine Research, P.O. Box 1870, 5020 Bergen, Norway; [email protected] (T.S.); [email protected] (P.A.J.P.); [email protected] (K.H.S.) * Correspondence: [email protected] These authors contributed equally to this work. y Received: 11 June 2020; Accepted: 23 July 2020; Published: 25 July 2020 Abstract: Selenium is an essential micronutrient and its metabolism is closely linked to the methionine cycle and transsulfuration pathway. The present study evaluated the effect of two different selenium supplements in the diet of rainbow trout (Onchorhynchus mykiss) broodstock on the one-carbon metabolism and the hepatic DNA methylation pattern in the progeny. Offspring of three parental groups of rainbow trout, fed either a control diet (NC, basal Se level: 0.3 mg/kg) or a diet supplemented with sodium selenite (SS, 0.8 mg Se/kg) or hydroxy-selenomethionine (SO, 0.7 mg Se/kg), were collected at swim-up fry stage. -
Modern Diversification of the Amino Acid Repertoire Driven by Oxygen
Modern diversification of the amino acid repertoire driven by oxygen Matthias Granolda, Parvana Hajievab, Monica Ioana Tos¸ac, Florin-Dan Irimiec, and Bernd Moosmanna,1 aEvolutionary Biochemistry and Redox Medicine, Institute for Pathobiochemistry, University Medical Center of the Johannes Gutenberg University, 55128 Mainz, Germany; bCellular Adaptation Group, Institute for Pathobiochemistry, University Medical Center of the Johannes Gutenberg University, 55128 Mainz, Germany; and cGroup of Biocatalysis and Biotransformations, Faculty of Chemistry and Chemical Engineering, Babes¸-Bolyai University, Cluj-Napoca 400028, Romania Edited by Harry B. Gray, California Institute of Technology, Pasadena, CA, and approved November 21, 2017 (received for review October 1, 2017) All extant life employs the same 20 amino acids for protein bio- aminoacyl-tRNA synthetases may not have been present in synthesis. Studies on the number of amino acids necessary to LUCA, the last universal common ancestor, but rather would have produce a foldable and catalytically active polypeptide have shown been distributed throughout life at a later time by lateral gene that a basis set of 7–13 amino acids is sufficient to build major struc- transfer (14). Similarly, the capacity to distinguish the late AA tural elements of modern proteins. Hence, the reasons for the evo- methionine from its genetic code neighbor isoleucine has probably lutionary selection of the current 20 amino acids out of a much larger developed only after the radiation of life (15). These observations available pool have remained elusive. Here, we have analyzed the call for selective factors behind the addition of methionine, Y, and quantum chemistry of all proteinogenic and various prebiotic amino W to the genetic code that have only become relevant to life acids.