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Selenoprotein

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https://www.readbyqxmd.com/read/28928140/selenoprotein-t-is-a-novel-ost-subunit-that-regulates-upr-signaling-and-hormone-secretion
#1
Abdallah Hamieh, Dorthe Cartier, Houssni Abid, André Calas, Carole Burel, Christine Bucharles, Cedric Jehan, Luca Grumolato, Marc Landry, Patrice Lerouge, Youssef Anouar, Isabelle Lihrmann
Selenoprotein T (SelT) is a recently characterized thioredoxin-like protein whose expression is very high during development, but is confined to endocrine tissues in adulthood where its function is unknown. We report here that SelT is required for adaptation to the stressful conditions of high hormone level production in endocrine cells. Using immunofluorescence and TEM immunogold approaches, we find that SelT is expressed at the endoplasmic reticulum membrane in all hormone-producing pituitary cell types. SelT knockdown in corticotrope cells promotes unfolded protein response (UPR) and ER stress and lowers endoplasmic reticulum-associated protein degradation (ERAD) and hormone production...
September 19, 2017: EMBO Reports
https://www.readbyqxmd.com/read/28917055/identification-of-genetic-disorders-causing-disruption-of-selenoprotein-biosynthesis
#2
Erik Schoenmakers, Krishna Chatterjee
Disorders of selenoprotein biosynthesis in humans, due to mutations in three genes (SECISBP2, TRU-TCA1-1, and SEPSECS) involved in the selenocysteine insertion pathway, have been described. Patients with SECISBP2 and TRU-TCA1-1 defects manifest a multisystem disorder with a biochemical signature of abnormal thyroid function tests due to the impaired activity of deiodinase selenoenzymes, myopathic features linked to SEPN1 deficiency and phenotypes resulting from increased levels of reactive oxygen species attributable to lack of antioxidant selenoenzymes...
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28917054/association-of-single-nucleotide-polymorphisms-in-selenoprotein-genes-with-cancer-risk
#3
Catherine Méplan
Genetic association studies have linked genetic variants in the Selenium (Se) metabolism with the development of complex diseases such as cancer and helped unravel novel mechanisms underlying cancer development. The chapter describes the specificity of genetic variants in the Se metabolism, the approaches used in association studies, and the limitations of such approaches.
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28917053/selective-evaluation-of-thioredoxin-reductase-enzymatic-activities
#4
Elias S J Arnér
Thioredoxin reductases are important oxidoreductases that keep the active site disulfide/dithiol motif of thioredoxins reduced using NADPH, thereby supporting many thioredoxin-dependent reductive pathways in cells. Mammalian thioredoxin reductases are selenoproteins that have several additional substrates beyond thioredoxins. This chapter first lists several different assays for measurement of thioredoxin reductase activities, before giving a protocol for a selective evaluation of these activities that can be used in either crude cell lysates as well as with purified enzymes...
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28917052/monitoring-of-methionine-sulfoxide-content-and-methionine-sulfoxide-reductase-activity
#5
Lionel Tarrago, Emmanuel Oheix, Zalán Péterfi, Vadim N Gladyshev
The sulfur-containing amino acid methionine (Met) plays critical roles in protein synthesis, methylation, and sulfur metabolism. Both in its free form and in the form of an amino acid residue, it can be oxidized to the R and S diastereomers of methionine sulfoxide (MetO). Organisms evolved methionine sulfoxide reductases (MSRs) to reduce MetO to Met, with the MSRs type A (MSRA) and type B (MSRB) being specific for the S and R forms of MetO, respectively. In mammals, the selenoprotein MSRB1 plays an important protein repair function, and its expression is tightly regulated by dietary selenium...
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28917051/selenocysteine-mediated-expressed-protein-ligation-of-selenom
#6
Jun Liu, Qingqing Chen, Sharon Rozovsky
A sizeable fraction of the selenoproteome encodes oxidoreductases possessing a thioredoxin fold, a structural motif that is shared among a diverse group of enzymes. In these oxidoreductases, the active site is comprised of a cysteine and a selenocysteine separated by one to two amino acids. In a subset of these selenoproteins, such as human SELENOH, SELENOM, SELENOT, SELENOV, SELENOW, and SELENOF, this redox motif is positioned immediately after the first β-sheet in a short loop, and is essential for interactions with its substrate or partners...
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28917050/preparation-of-selenocysteine-containing-forms-of-human-selenok-and-selenos
#7
Zhengqi Zhang, Jun Liu, Sharon Rozovsky
Selenoprotein K (SELENOK) and Selenoprotein S (SELENOS) are the members of the endoplasmic-reticulum-associated degradation (ERAD) complex, which is responsible for translocating misfolded proteins from the endoplasmic reticulum (ER) to the cytosol for degradation. Besides its involvement in the ERAD, SELENOK was shown to bind and stabilize the palmitoyl transferase DHHC6, and thus contributes to palmitoylation. SELENOK and SELENOS reside in the ER membrane by the way of a single transmembrane helix. Both contain an intrinsically disordered region with a selenocysteine (Sec) located one or two residues away from the C-terminus...
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28917049/overexpression-of-recombinant-selenoproteins-in-e-coli
#8
Qing Cheng, Elias S J Arnér
Expression of selenoproteins necessitates a process of decoding of a UGA codon from termination of translation to insertion of selenocysteine. The mechanisms of this process pose major challenges with regards to recombinant selenoprotein production in E. coli, which however can be overcome especially if the Sec residue is located close to the C-terminal end, as is the case for several naturally found selenoproteins. This chapter summarizes a method to achieve such a production.
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28917048/imaging-of-selenium-by-laser-ablation-inductively-coupled-plasma-mass-spectrometry-la-icp-ms-in-2-d-electrophoresis-gels-and-biological-tissues
#9
Elisa Castañeda Santa Cruz, J Susanne Becker, J Sabine Becker, Alessandra Sussulini
Selenium and selenoproteins are important components of living organisms that play a role in different biological processes. Laser ablation inductively coupled plasma mass spectrometry (LA-ICP-MS) is a powerful analytical technique that has been employed to obtain distribution maps of selenium in biological tissues in a direct manner, as well as in selenoproteins, previously separated by their molecular masses and isoelectric points using two-dimensional polyacrylamide gel electrophoresis (2-D PAGE). In this chapter, we present the protocols to perform LA-ICP-MS imaging experiments, allowing the distribution visualization and determination of selenium and/or selenoproteins in biological systems...
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28917047/detection-of-selenoproteins-by-laser-ablation-inductively-coupled-plasma-mass-spectrometry-la-icp-ms-in-immobilized-ph-gradient-ipg-strips
#10
Jordan Sonet, Sandra Mounicou, Laurent Chavatte
In contrast to other trace elements that are cofactors of enzymes and removed from proteins under denaturing conditions, Se is covalently bound to proteins when incorporated into selenoproteins, since it is a component of selenocysteine aminoacid. It implies that selenoproteins can undergo several biochemical separation methods in stringent and chaotropic conditions and still maintain the presence of selenium in the primary sequence. This feature has been used to develop a method for the detection of trace levels of human selenoproteins in cell extracts without the use of radioactive isotopes...
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28917046/nonradioactive-isotopic-labeling-and-tracing-of-selenoproteins-in-cultured-cell-lines
#11
Jordan Sonet, Sandra Mounicou, Laurent Chavatte
Selenium (Se) is an essential component of genetically encoded selenoproteins, in the form of a rare amino acid, namely the selenocysteine (Sec). Radioactive (75)Se has been widely used to trace selenoproteins in vitro and in vivo (cell models and animals). Alternatively, its unique isotopic pattern can be used to detect and characterize nonradioactive Se-compounds in cellular extracts using molecular or elemental mass spectrometry at ppm levels. However, when studying trace levels of Se-compounds, such as selenoproteins (ppt levels), the distribution of the signal between its six naturally abundant isotopes reduces its sensitivity...
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28917045/radioactive-75-se-labeling-and-detection-of-selenoproteins
#12
Sun Hee Yim, Ryuta Tobe, Anton A Turanov, Bradley A Carlson
The trace element selenium (Se) is incorporated into proteins as the amino acid selenocysteine (Sec), which is cotranslationally inserted into specific proteins in response to a UGA codon. Proteins containing Sec at these specific positions are called selenoproteins. Most selenoproteins function as oxidoreductases, while some serve other important functions. There are 25 known selenoprotein genes in humans and 24 in mice. The use of Sec allows selenoproteins to be detected by a convenient method involving metabolic labeling with (75)Se...
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28917044/simultaneous-speciation-of-selenoproteins-and-selenometabolites-in-plasma-and-serum
#13
Belén Callejón-Leblic, Gema Rodríguez-Moro, Tamara García-Barrera, José Luis Gómez-Ariza
Selenium is an essential element incorporated to different proteins with important biological functions in connection to antioxidant activity, cancer-protective properties, neurodegenerative pathologies, and prevention of effects of diabetes, among others. In addition, selenoamino acids play a basic role in the global equilibrium of key selenium-biomolecules synthesis, including selenoprotein P, selenoalbumin, and glutathione peroxidase. Homeostasis of these selenium-containing biomolecules involves different organs in living organisms including human, and bloodstream is the connection fluid in this process...
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28917041/modification-of-selenoprotein-mrnas-by-cap-tri-methylation
#14
Anne-Sophie Gribling-Burrer, Gilbert Eriani, Christine Allmang
Several selenoprotein mRNAs undergo 5' cap maturation events whereby their classical monomethylated m(7)G cap becomes trimethylated (m3(2,2,7)G) by the trimethylguanosine synthase 1 (Tgs1). Here, we describe immunoprecipitation methods for the detection of endogenous m3(2,2,7)G-capped selenoprotein mRNAs from total cell extracts or after polysome fractionation of cytoplasmic extracts. We have also developed a method for the in vitro cap hypermethylation of selenoprotein mRNA transcripts using purified Tgs1 enzyme...
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28917040/studying-selenoprotein-mrna-translation-using-rna-seq-and-ribosome-profiling
#15
Brian K Dalley, Lisa Baird, Michael T Howard
Deep sequencing of ribosome protected mRNA footprints, also called ribosome profiling or Ribo-Seq, is a relatively new methodology well suited to address questions regarding the mechanisms and efficiency of protein expression. Specifically, the ability of this technique to quantify ribosome abundance with codon resolution enables experiments aimed at studying many aspects of translation, including gene-specific translational efficiency, translation of regulatory upstream short open reading frames, sites of ribosome pausing, and most importantly for selenoproteins, the efficiency by which UGA codons are redefined to encode selenocysteine...
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28917038/specific-chemical-approaches-for-studying-mammalian-ribosomes-complexed-with-ligands-involved-in-selenoprotein-synthesis
#16
Olga Kossinova, Alexey Malygin, Alain Krol, Galina Karpova
Chemical approaches are very powerful tools for investigating the molecular structure and architecture of large ribonucleoprotein complexes involving ribosomes and other components of the translation system. Application of RNA nucleotide-specific and cross-linking reagents of a broad specificity range allows the researcher to obtain information on the sites of ligand binding to the ribosome and to each other as well as on the RNA rearrangements caused by the binding. Here, we describe specific chemical approaches including chemical probing and site-directed or bifunctional reagent-mediated cross-linking, which have been used for exploring the mechanism of selenocysteine insertion into a polypeptide chain by mammalian ribosomes...
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28917037/identification-and-characterization-of-proteins-that-bind-to-selenoprotein-3-utrs
#17
Eric M Cockman, Donna M Driscoll
This chapter explains the use of RNase-assisted RNA chromatography. RNA affinity chromatography is a powerful technique that is used to isolate and identify proteins that bind to a specific RNA ligand. The RNA of interest is attached to beads before protein lysates are passed over the column. In traditional RNA chromatography, bound proteins are eluted with high salt or harsh detergent, which can also release proteins that are nonspecifically bound to the beads. To avoid this, a new method was developed in which RNases are used to cleave RNA from the beads, releasing only RNA binding proteins (RBPs) and leaving behind proteins that are bound to the beads (Michlewski and Caceres, RNA 16(8):1673-1678, 2010)...
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28917036/selenocysteine-trna-ser-sec-the-central-component-of-selenoprotein-biosynthesis-isolation-identification-modification-and-sequencing
#18
Bradley A Carlson, Byeong Jae Lee, Petra A Tsuji, Paul R Copeland, Ulrich Schweizer, Vadim N Gladyshev, Dolph L Hatfield
The selenocysteine (Sec) tRNA([Ser]Sec) population consists of two isoforms that differ from each other by a single 2'-O-methylribosyl moiety at position 34 (Um34). These two isoforms, which are encoded in a single gene, Trsp, and modified posttranscriptionally, are involved individually in the synthesis of two subclasses of selenoproteins, designated housekeeping and stress-related selenoproteins. Techniques used in obtaining these isoforms for their characterization include extraction of RNA from mammalian cells and tissues, purifying the tRNA([Ser]Sec) population by one or more procedures, and finally resolving the two isoforms from each other...
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28917035/selgenamic-an-algorithm-for-selenoprotein-gene-assembly
#19
Liang Jiang, Qiong Liu
Computational methods for identifying selenoproteins have been developed rapidly in recent years. However, it is still difficult to identify the open reading frame (ORF) of eukaryotic selenoprotein gene, because the TGA codon for a selenocysteine (Sec) residue in the active center of selenoprotein is traditionally a terminal signal of protein translation. A gene assembly algorithm SelGenAmic has been constructed and presented in this chapter for identifying selenoprotein genes from eukaryotic genomes. A method based on this algorithm was developed to build an optimal TGA-containing-ORF for each TGA in a genome, followed by protein similarity analysis through conserved sequence alignments to screen out selenoprotein genes from these ORFs...
2018: Methods in Molecular Biology
https://www.readbyqxmd.com/read/28917034/selenoprofiles-a-computational-pipeline-for-annotation-of-selenoproteins
#20
Didac Santesmasses, Marco Mariotti, Roderic Guigó
Selenoproteins contain selenocysteine (Sec or U), the 21st amino acid, inserted in response to an in-frame UGA codon. UGA normally terminates translation, but in selenoprotein mRNAs it is recoded to specify Sec insertion. For this reason, standard gene prediction programs fail to predict Sec codons, and selenoproteins are usually misannotated in protein databases and genome projects. Selenoprofiles is a computational pipeline able to correctly annotate selenoprotein genes in genomic sequences. This program uses a SECIS-independent approach, based on homology searches, and employs curated built-in profile alignments for all known selenoprotein families...
2018: Methods in Molecular Biology
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