Selenoprotein Structure and Function
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Selenoprotein Structure and Function

1st Edition - January 28, 2022

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  • Editor: Eranthie Weerapana
  • eBook ISBN: 9780323907361
  • Hardcover ISBN: 9780323907354

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Description

Selenoprotein Structure and Function, Volume 662 in the Methods in Enzymology series, highlights new advances in the field, with this new volume presenting interesting chapters written by an international board of authors. Chapters in this new release include Identification of Selenoprotein O substrates using a biotinylated ATP analog, Selenium-encoded isotopic signature targeted profiling, Designing tRNASec variants for efficient selenocysteine incorporation using Sec-specific reporters, Preparation of selenoprotein S by chemical ligation, Examining xCT-mediated selenium uptake and selenoprotein production capacity in cells, SecMS analysis of selenoprotein with selenocysteine insertion sequence and beyond, Selenocysteine substitutions in thiyl radical enzymes, and much more. Additional chapters cover Recombinant selenoprotein expression in E. coli based upon the redefinition of a UAG codon in an RF1-depleted host strain, Metabolic labeling with radioactive selenium in zebrafish, Low pH isoTOP-ABPP to identify selenocysteines, Expression of selenoproteins via genetic code expansion in mammalian cells, Alpha-methyl selenocysteine as a tool for the study of selenoproteins, Selective selenol fluorescent probes: design, synthesis, structural determinants, and biological applications, and much more.

Key Features

  • Provides the authority and expertise of leading contributors from an international board of authors
  • Presents the latest release in the Methods in Enzymology series
  • Updated release includes the latest information on Selenoprotein Structure and Function

Readership

Biochemists, biophysicists, molecular biologists, analytical chemists, and physiologists

Table of Contents

  • Cover image
  • Title page
  • Table of Contents
  • Copyright
  • Contributors
  • Preface
  • Chapter One: Examining xCT-mediated selenium uptake and selenoprotein production capacity in cells
  • Abstract
  • 1: Introduction
  • 2: Measurement of selenium uptake and selenoprotein production as mediated by xCT transporter
  • 3: Summary
  • Acknowledgment
  • References
  • Chapter Two: Methods for accurate and reproducible studies of pharmacological effects of selenium in cancer
  • Abstract
  • 1: Introduction
  • 2: Selenium cytotoxicity in cancer cell lines
  • 3: Metabolites and selenoproteins in plasma and serum after administration of pharmacological high doses of selenite IV
  • 4: Mammalian thioredoxin reductase (TrxR, TR, TXNRD) assay
  • 5: KYAT determination
  • 6: Selenium treatment and microRNA expression
  • 7: Selenium and the immune system
  • 8: Concluding remarks
  • Acknowledgments
  • Conflicts of interest
  • References
  • Chapter Three: Using selenocysteine-specific reporters to screen for efficient tRNASec variants
  • Abstract
  • 1: Introduction
  • 2: Natural selenocysteine translation
  • 3: Recombinant selenocysteine translation
  • 4: Evolving tRNASec variants for increased Sec incorporation
  • 5: Protocol
  • 6: Expected outcomes
  • 7: Advantages
  • 8: Limitations
  • 9: Optimization and troubleshooting
  • Acknowledgments
  • Funding
  • References
  • Chapter Four: Expressing recombinant selenoproteins using redefinition of a single UAG codon in an RF1-depleted E. coli host strain
  • Abstract
  • 1: Introduction
  • 2: Selenoprotein production
  • 3: Using UAG redefinition as a sec codon in an RF1-depleted E. coli host strain
  • 4: Materials
  • 5: Protocol
  • 6: Selenoprotein analysis and quality assessment
  • 7: Concluding remarks
  • Acknowledgments
  • Conflict of interests
  • References
  • Chapter Five: Selenocysteine substitutions in thiyl radical enzymes
  • Abstract
  • 1: Introduction
  • 2: Recombinant expression of selenoproteins by non-sense suppression
  • 3: Assembling pCm-based vectors and optimizing selenoprotein expression
  • 4: Milligram scale selenoprotein preparation
  • 5: Evaluating the effect of cysteine-to-selenocysteine substitution
  • Acknowledgments
  • References
  • Chapter Six: Expression of selenoproteins via genetic code expansion in mammalian cells
  • Abstract
  • 1: Introduction
  • 2: Methods
  • 3: Conclusions and outlooks
  • References
  • Chapter Seven: Applying selenocysteine-mediated expressed protein ligation to prepare the membrane enzyme selenoprotein S
  • Abstract
  • 1: Introduction
  • 2: Considerations for Sec-mediated EPL using selenopeptides
  • 3: Materials
  • 4: Protocol
  • 5: Analysis of the product
  • 6: Summary
  • Acknowledgments
  • References
  • Chapter Eight: Chemoproteomic interrogation of selenocysteine by low-pH isoTOP-ABPP
  • Abstract
  • 1: Introduction
  • 2: Technical aspects
  • 3: Results and discussion
  • References
  • Chapter Nine: SecMS analysis of selenoproteins with selenocysteine insertion sequence and beyond
  • Abstract
  • 1: Introduction
  • 2: SecMS and SIS database
  • 3: Materials
  • 4: Protocols
  • 5: Summary
  • Acknowledgment
  • References
  • Chapter Ten: An accelerated and optimized algorithm of selenium-encoded isotopic signature targeted profiling for global selenoproteome analysis
  • Abstract
  • 1: Introduction
  • 2: Targeted proteomic profiling and SESTAR
  • 3: SESTAR ++: Accelerated SESTAR algorithm
  • 4: Method
  • 5: Summary
  • Acknowledgment
  • References
  • Chapter Eleven: Assay of selenol species in biological samples by the fluorescent probe Sel-green
  • Abstract
  • 1: Introduction
  • 2: Fluorescent probe for Sec
  • 3: In vitro characterization of probes
  • 4: Detection of Sec in live cells
  • 5: Conclusions
  • Acknowledgments
  • References
  • Chapter Twelve: Identification of selenoprotein O substrates using a biotinylated ATP analog
  • Abstract
  • 1: Introduction
  • 2: Key resources table
  • 3: Materials and equipment
  • 4: Step-by-step method details
  • 5: Expected outcomes
  • 6: Advantages
  • 7: Limitations
  • 8: Optimization and troubleshooting
  • 9: Safety considerations and standards
  • 10: Alternative methods/procedures
  • Acknowledgments
  • References
  • Chapter Thirteen: Application of alpha-methyl selenocysteine as a tool for the study of selenoproteins
  • Abstract
  • 1: Introduction
  • 2: Materials and methods
  • 3: Results and discussion
  • 4: Conclusions
  • References
  • Chapter Fourteen: Modeling of selenocysteine-derived reactive intermediates utilizing a nano-sized molecular cavity as a protective cradle
  • Abstract
  • 1: Introduction
  • 2: Molecular design for stabilization of selenocysteine-derived reactive species
  • 3: Modeling the catalytic cycle of GPx by NMR spectroscopic analysis of Sec–SeOHs
  • 4: Protocol
  • 5: Conclusion
  • Acknowledgments
  • References
  • Chapter Fifteen: Diselenide-selenoester ligation in the chemical synthesis of proteins
  • Abstract
  • 1: Introduction
  • 2: Advent of DSL
  • 3: General DSL and rDSL protocols
  • 4: Assembly of proteins through ligations at challenging junctions
  • 5: Rapid and selective deselenization
  • 6: Protein assembly via one-pot iterative DSL reactions
  • 7: Summary
  • Acknowledgments
  • References

Product details

  • No. of pages: 416
  • Language: English
  • Copyright: © Academic Press 2022
  • Published: January 28, 2022
  • Imprint: Academic Press
  • eBook ISBN: 9780323907361
  • Hardcover ISBN: 9780323907354

About the Serial Volume Editor

Eranthie Weerapana

Eranthie Weerapana is an Associate Professor of Chemistry at Boston College. She received her B.S. in Chemistry from Yale University, and her Ph.D. in Chemistry from MIT, where she worked with Professor Barbara Imperiali, investigating glycosyltransferases involved in N-linked glycosylation in the gram negative bacterium Campylobacter jejuni. She then performed postdoctoral studies at The Scripps Research Institute, La Jolla where she worked with Professor Benjamin F. Cravatt to develop chemical-proteomic methods to investigate reactive cysteines in complex proteomes. Her interdisciplinary research program focuses on applying mass-spectrometry methods to identify regulatory cysteine residues in the human proteome, and chemical biology approaches to develop covalent small-molecule modulators for cysteine-mediated protein activities.

Affiliations and Expertise

Associate Professor of Chemistry Chemistry Department Faculty Morrissey College of Arts and Sciences Boston College

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