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Gas sensing in cells PDF

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Gas Sensing in Cells 1 0 0 P F 6- 3 8 2 1 0 8 8 7 1 8 7 9 9/ 3 0 1 0. 1 oi: d g | or c. s s.r b u p p:// htt n o 7 1 0 2 er b o ct O 1 3 n o d e h s bli u P View Online Metallobiology Series Editor-in-chief: C. David Garner, University of Nottingham, UK 1 0 0 P Series editors: F 36- Stefano L. Ciurli, University of Bologna, Italy 8 12 Hongzhe Sun, University of Hong Kong, China 0 88 Anthony Wedd, University of Melbourne, Australia 7 81 Julie Kovacs, University of Washington, USA 7 9 9/ 3 0 Titles in the Series: 1 10. 1: Mechanisms and Metal Involvement in Neurodegenerative Diseases doi: 2: Binding, Transport and Storage of Metal Ions in Biological Cells g | 3: 2-Oxoglutarate-Dependent Oxygenases or c. 4: Heme Peroxidases s bs.r 5: Molybdenum and Tungsten Enzymes: Biochemistry u http://p 67:: M Moollyybbddeennuumm aanndd T uTunngsgtsetnen E nEznyzmymese: sB: ioSipneocrtgraonscico pCihce manisdt rTyheoretical n Investigations o 17 8: Metal Chelation in Medicine 0 er 2 9: Metalloenzymes in Denitrification: Applications and Environmental ob Impacts ct O 10: The Biological Chemistry of Nickel 1 3 11: Gas Sensing in Cells n o d e h s bli u P How to obtain future titles on publication: A standing order plan is available for this series. A standing order will bring delivery of each new volume immediately on publication. For further information please contact: Book Sales Department, Royal Society of Chemistry, Thomas Graham House, Science Park, Milton Road, Cambridge, CB4 0WF, UK Telephone: +44 (0)1223 420066, Fax: +44 (0)1223 420247, Email: [email protected] Visit our website at www.rsc.org/books View Online Gas Sensing in Cells 1 0 0 P F 6- Edited by 3 8 2 1 80 Shigetoshi Aono 8 7 1 Okazaki Institute for Integrative Bioscience, Institute for Molecular Science, 8 7 9 Japan 9/ 03 Email: [email protected] 1 0. 1 oi: d g | or c. s s.r b u p p:// htt n o 7 1 0 2 er b o ct O 1 3 n o d e h s bli u P View Online 1 0 0 P F 6- 3 8 2 1 0 8 8 7 1 8 97 Metallobiology Series No. 11 9/ 3 0 1 Print ISBN: 978-1-78262-895-8 0. 1 PDF ISBN: 978-1-78801-283-6 doi: EPUB ISBN: 978-1-78801-343-7 g | ISSN: 2045-547X or c. s s.r A catalogue record for this book is available from the British Library b u p p:// © The Royal Society of Chemistry 2018 htt n All rights reserved o 7 1 20 Apart from fair dealing for the purposes of research for non-commercial purposes or for er private study, criticism or review, as permitted under the Copyright, Designs and Patents b o ct Act 1988 and the Copyright and Related Rights Regulations 2003, this publication may O 1 not be reproduced, stored or transmitted, in any form or by any means, without the prior 3 n permission in writing of The Royal Society of Chemistry or the copyright owner, or in o d the case of reproduction in accordance with the terms of licences issued by the Copyright e sh Licensing Agency in the UK, or in accordance with the terms of the licences issued by the ubli appropriate Reproduction Rights Organization outside the UK. Enquiries concerning P reproduction outside the terms stated here should be sent to The Royal Society of Chemistry at the address printed on this page. Whilst this material has been produced with all due care, The Royal Society of Chemistry cannot be held responsible or liable for its accuracy and completeness, nor for any consequences arising from any errors or the use of the information contained in this publication. The publication of advertisements does not constitute any endorsement by The Royal Society of Chemistry or Authors of any products advertised. The views and opinions advanced by contributors do not necessarily reflect those of The Royal Society of Chemistry which shall not be liable for any resulting loss or damage arising as a result of reliance upon this material. The Royal Society of Chemistry is a charity, registered in England and Wales, Number 207890, and a company incorporated in England by Royal Charter (Registered No. RC000524), registered office: Burlington House, Piccadilly, London W1J 0BA, UK, Telephone: +44 (0) 207 4378 6556. For further information see our web site at www.rsc.org Printed in the United Kingdom by CPI Group (UK) Ltd, Croydon, CR0 4YY, UK 5 0 0 P F 6- 3 Preface 8 2 1 0 8 8 7 1 8 7 9 9/ 3 0 1 0. Gas molecules are well known as substrates/products of enzymes in a variety 1 oi: of biological reactions including respiration, denitrification, photosynthe- d g | sis, methanogenesis, and several other metabolism/catabolism systems. It or c. has become apparent that they also act as signalling molecules to regulate s s.r their biological activities in all living organisms. In the late 1980s, nitric b u p oxide (NO) was shown to act as the mediator of endothelium-derived relax- p:// ing factor via the activation of an NO receptor (soluble guanylate cyclase) by htt n a nitrosyl–haem complex. The Nobel Prize in Physiology or Medicine 1998 o 7 was awarded jointly to Robert F. Furchgott, Louis J. Ignarro and Ferid Murad 1 0 2 “for their discoveries concerning nitric oxide as a signalling molecule in the er b cardiovascular system”. o Oct In the late 1990s carbon monoxide (CO) was confirmed to act as a physio- 31 logical effector of a bacterial transcriptional regulator CooA employing haem n o to sense CO and before that it was reported that haem acts as a molecular d he oxygen (O ) sensor in FixL, a histidine kinase in the FixL/FixJ two-component s 2 bli system responsible for the regulation of O -dependent gene expression. In u 2 P 2000, haem-based O -sensors HemATs were identified in aerotaxis regulatory 2 systems, which are chemotaxis signal transducer proteins directly sensing O . Though it had been well known that molecular oxygen controls the met- 2 abolic switch between respiration and fermentation in facultative anaerobes such as Escherichia coli, the molecular mechanism of the metabolic switch was unknown. In the 1990s and later, FNR was identified as a master switch whose function is regulated by O . A protein-bound iron–sulfur cluster acts 2 as the O sensor. Recently, it was verified that iron–sulfur clusters act as NO 2 sensors as well.   Metallobiology Series No. 11 Gas Sensing in Cells Edited by Shigetoshi Aono © The Royal Society of Chemistry 2018 Published by the Royal Society of Chemistry, www.rsc.org v View Online vi Preface Though the first report suggesting that ethylene functions as a plant hor- mone dates back to 1896, developments of research on ethylene signalling had to wait for the introduction of molecular biology techniques and the model plant, Arabidopsis thaliana. An ethylene receptor was cloned in 1988 5 for the first time and 16 genes related to ethylene signalling have been iden- 0 P0 tified in Arabidopsis thaliana. Cu(i) is proposed as the active site for sensing F 6- ethylene in ethylene receptors. 3 28 The numbers of gas-sensor proteins identified and characterized are 1 80 increasing partly because of the expansion of genomic data and develop- 8 17 ment of experimental techniques including X-ray crystallography and cer- 8 97 tain spectroscopies. Metal-containing prosthetic groups are good probes 9/ 3 for spectroscopic measurements that enables elucidation of the structural 0 1 0. and functional relationships of active sites in gas-sensor proteins at atomic/ 1 oi: molecular levels. This book focuses on recent developments in research on d g | gas sensor systems. Haem-, iron–sulfur cluster- and nonhaem iron-based c.or gas-sensor proteins are surveyed in Chapters 2–6 and mammalian O2 and s s.r plant ethylene signalling systems in Chapters 7 and 8, respectively. b pu I would like to thank the authors of each of the chapters in this book for p:// their efforts in preparing the comprehensive and up-to-date chapters. Finally, n htt I would like to express my gratitude to Anthony G. Wedd for his encourage- o 7 ment, advice, and help in preparing this book. 1 0 2 er Shigetoshi Aono b o ct O 1 3 n o d e h s bli u P 7 0 0 P F 6- 3 Contents 8 2 1 0 8 8 7 1 8 7 9 9/ 3 0 1 0. Chapter 1 Overview of Gas-sensing Systems 1 1 oi: Shigetoshi Aono d g | or c. 1.1 Introduction 1 s s.r 1.2 Biological Signal-transduction Systems b u p Including Gas Sensing 2 p:// 1.2.1 Single-component Systems 2 htt n 1.2.2 Two-component Systems 2 o 7 1.2.3 Multicomponent Systems 6 1 0 2 1.3 Prosthetic Groups Utilized to Sense Gas Molecules 7 er b 1.3.1 Haem 7 o Oct 1.3.2 Iron–Sulfur Clusters 8 31 1.3.3 Nonhaem Iron Centres 9 n o References 11 d e h s bli Chapter 2 Haem-based Sensors of Nitric Oxide 15 u P D. E. Williams, J. T. Fischer, I. Heckler and E. M. Boon 2.1 Introduction 15 2.2 The Mammalian NO Sensor: Soluble Guanylyl Cyclase (sGC) 17 2.3 Bacterial NO-sensing H-NOX Proteins 19 2.3.1 Discovery of the H-NOX Family 19 2.3.2 Operon Organization of H-NOX Proteins 20 2.3.3 Ligand-binding Properties of H-NOX Proteins 21 2.3.4 Structural Characterization of H-NOX Proteins 22   Metallobiology Series No. 11 Gas Sensing in Cells Edited by Shigetoshi Aono © The Royal Society of Chemistry 2018 Published by the Royal Society of Chemistry, www.rsc.org vii View Online viii Contents 2.3.5 Hydrogen Bonding Through a Tyrosine Residue in the Distal Pocket Facilitates Ligand Discrimination 23 2.3.6 H-NOX Haem Distortion and Its Role in 7 Signal Transduction 24 0 P0 2.3.7 Iron–Histidine Bond Cleavage Upon NO F 6- Binding Leads to Haem Relaxation 26 3 28 2.3.8 Ligand Migration Through the H-NOX 1 80 Tunnel System 29 8 17 2.4 The YybT Family of Haem–PAS Domains 29 8 97 2.4.1 Discovery That YybT is a Haemoprotein 9/ 3 Family 30 0 1 0. 2.4.2 Evidence That YybT is an NO Sensor 31 1 oi: 2.5 The E75 Family of Haem-bound Transcription d g | Factors 32 c.or 2.5.1 Characterization of E75 in Drosophila s s.r melanogaster 33 b pu 2.5.2 Rev-erbs: Mammalian Homologues of E75 34 p:// 2.6 Haem and NO Signalling in Regulating Biofilm n htt Formation in Pseudomonas aeruginosa 35 o 7 2.6.1 NO Regulation of Biofilm Formation in 1 20 P. aeruginosa 35 ber 2.6.2 The Discovery of a Novel Bacterial o ct NO-sensing Protein (NosP) 36 O 1 2.7 DNR: Transcriptional Regulator of Denitrification 36 3 on 2.7.1 Protein Structure of Inactive and Active DNR 37 d e 2.7.2 Ligand-binding Properties of DNR 38 h s bli 2.7.3 Activation of DNR by NO 39 u P 2.8 Conclusions and Perspectives 39 References 41 Chapter 3 Haem-based Sensors of Dioxygen 47 Hitomi Sawai and Yoshitsugu Shiro 3.1 Introduction 47 3.2 Variations in the Sensor Domain of Haem-based O -sensor Proteins 49 2 3.2.1 PAS Domain 49 3.2.2 GAF Domain 50 3.2.3 GCS Domain 50 3.3 Two-component Signal Transduction Regulated by O Sensing 51 2 3.3.1 FixL 52 3.3.2 DevS (DosS) and DosT 57 3.3.3 Af GcHK 59 View Online Contents ix 3.4 Aerotaxis Control for the Regulation of Bacterial Flagellar Rotation 61 3.4.1 HemAT 62 3.4.2 Aer2 63 7 3.5 Synthesis and Hydrolysis of Nucleotide Second 0 P0 Messengers 66 F 6- 3.5.1 YddV (DosC) and EcDOS (DosP) 68 3 28 3.5.2 HemDGC 71 1 80 3.5.3 AvGReg and BpeGReg 73 8 17 3.5.4 AxPDEA1 73 8 97 3.5.5 Atypical sGCs: Gyc-88E and GCY-35 73 9/ 3 3.5.6 HemAC-Lm 76 0 1 0. 3.6 Conclusions 78 1 oi: References 79 d g | c.or Chapter 4 Haem-based Sensors of Carbon Monoxide 84 s s.r Shigetoshi Aono b u p p:// 4.1 Introduction 84 n htt 4.2 Biological Production of CO 85 o 7 4.2.1 Endogenous CO Production for Ligand 1 20 of the Metal Clusters in Hydrogenases 85 ber 4.2.2 Endogenous CO Production by o ct Haemoxygenases 87 O 1 4.3 Biological Utilization of CO 89 3 on 4.3.1 Ni/Fe CO Dehydrogenase 89 d e 4.3.2 Mo/Cu CO Dehydrogenase 91 h s bli 4.4 Bacterial CO-sensor Protein CooA 92 u P 4.4.1 Structure of CooA 94 4.4.2 Allosteric Control of CRP as a Model of CooA 95 4.4.3 Allosteric Control of CooA by CO 99 4.4.4 Coordination Structures of the Haem in CooA 102 4.4.5 Redox Properties of the Haem in CooA 104 4.4.6 Spectroscopic Properties of the Haem in CooA 105 4.4.7 Ligand Discrimination of CooA 106 4.4.8 CO-binding Kinetics of CooA 107 4.4.9 DNA Binding and Transcriptional Activation of CooA 108 4.5 Bacterial CO-sensor Protein RcoM 110 4.5.1 PAS Domain in RcoM 110 4.5.2 Spectroscopic Properties of the PAS Domain in RcoM 111 View Online x Contents 4.5.3 Coordination Structure of the Haem in RcoM 111 4.5.4 CO-binding Kinetics of RcoM 113 4.5.5 LytTR Domain as a DNA-binding Motif 113 7 4.5.6 DNA Binding of LytTR Domain 114 0 P0 4.6 Mammalian CO-sensor Proteins NPAS2 and F 6- CLOCK 115 3 28 4.6.1 Structure of CLOCK/BMAL1 bHLH-PAS 1 80 Domains 116 8 17 4.6.2 DNA Binding of bHLH Domain 116 8 97 4.6.3 Haem as a CO Sensor in the PAS 9/ 3 Domains of NPAS2 and CLOCK 118 0 1 0. 4.6.4 Spectroscopic Properties of the Haem 1 oi: in NPAS2 and CLOCK 119 d g | 4.7 Mammalian Cystathionine β-synthase (CBS) 121 c.or 4.7.1 Structural and Spectroscopic Properties s s.r of the Haem in CBS 121 b pu 4.7.2 Ligand Binding Properties of CBS 123 p:// 4.7.3 Allosteric Control of CBS by CO 124 n htt 4.8 Concluding Remarks 125 o 7 Acknowledgements 126 1 20 References 126 er b o ct Chapter 5 Iron–Sulfur Cluster-based Sensors 136 O 1 Jason C. Crack and Nick E. Le Brun 3 n o d e 5.1 Introduction 136 h s ubli 5.2 O2-sensing Iron–Sulfur Cluster Proteins 139 P 5.2.1 FNR 139 5.2.2 NreB 149 5.2.3 AirS 150 5.3 Iron–Sulfur Cluster Proteins that Sense Reduced O (Reactive Oxygen Species) 150 2 5.3.1 SoxR 151 5.3.2 IscR 154 5.3.3 RsrR 155 5.4 Iron–Sulfur Cluster Proteins that Sense Nitric Oxide (NO) 156 5.4.1 NsrR 157 5.4.2 WhiB-like (Wbl) [4Fe–4S] Cluster- containing Regulatory Protein Family in Actinobacteria 163 5.4.3 FNR and FnrP 165 5.4.4 SoxR 166 5.4.5 Iron Regulatory Protein 1 (IRP1) 166 5.4.6 Corynebacterium glutamicum ArnR 168

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