Gas sensing in cells

✍ Scribed by Aono, Shigetoshi

• Publisher: Royal Society of Chemistry
• Year: 2018
• Tongue: English
• Leaves: 314
• Series: RSC metallobiology series 11
• Category: Library

✦ Synopsis

This book provides the first comprehensive overview of gas sensing in living cells and describes a wide spectrum of proteins that produce, sense or use gas molecules in both prokaryotic and eukaryotic cells.

Abstract:

This book provides the first comprehensive overview of gas sensing in living cells and describes a wide spectrum of proteins that produce, sense or use gas molecules in both prokaryotic and eukaryotic cells.  Read more...

✦ Table of Contents

Content: Machine generated contents note: ch. 1 Overview of Gas-sensing Systems / Shigetoshi Aono --
1.1.Introduction --
1.2.Biological Signal-transduction Systems Including Gas Sensing --
1.2.1.Single-component Systems --
1.2.2.Two-component Systems --
1.2.3.Multicomponent Systems --
1.3.Prosthetic Groups Utilized to Sense Gas Molecules --
1.3.1.Haem --
1.3.2.Iron-Sulfur Clusters --
1.3.3.Nonhaem Iron Centres --
References --
ch. 2 Haem-based Sensors of Nitric Oxide / E. M. Boon --
2.1.Introduction --
2.2.The Mammalian NO Sensor: Soluble Guanylyl Cyclase (sGC) --
2.3.Bacterial NO-sensing H-NOX Proteins --
2.3.1.Discovery of the H-NOX Family --
2.3.2.Operon Organization of H-NOX Proteins --
2.3.3.Ligand-binding Properties of H-NOX Proteins --
2.3.4.Structural Characterization of H-NOX Proteins --
2.3.5.Hydrogen Bonding Through a Tyrosine Residue in the Distal Pocket Facilitates Ligand Discrimination --
2.3.6.H-NOX Haem Distortion and Its Role in Signal Transduction Note continued: 2.3.7.Iron --
Histidine Bond Cleavage Upon NO Binding Leads to Haem Relaxation --
2.3.8.Ligand Migration Through the H-NOX Tunnel System --
2.4.The YybT Family of Haem --
PAS Domains --
2.4.1.Discovery That YybT is a Haemoprotein Family --
2.4.2.Evidence That YybT is an NO Sensor --
2.5.The E75 Family of Haem-bound Transcription Factors --
2.5.1.Characterization of E75 in Drosophila melanogaster --
2.5.2.Rev-erbs: Mammalian Homologues of E75 --
2.6.Haem and NO Signalling in Regulating Biofilm Formation in Pseudomonas aeruginosa --
2.6.1.NO Regulation of Biofilm Formation in P. aeruginosa --
2.6.2.The Discovery of a Novel Bacterial NO-sensing Protein (NosP) --
2.7.DNR: Transcriptional Regulator of Denitrification --
2.7.1.Protein Structure of Inactive and Active DNR --
2.7.2.Ligand-binding Properties of DNR --
2.7.3.Activation of DNR by NO --
2.8.Conclusions and Perspectives --
References --
ch. 3 Haem-based Sensors of Dioxygen / Yoshitsugu Shiro Note continued: 3.1.Introduction --
3.2.Variations in the Sensor Domain of Haem-based O2-sensor Proteins --
3.2.1.PAS Domain --
3.2.2.GAF Domain --
3.2.3.GCS Domain --
3.3.Two-component Signal Transduction Regulated by O2 Sensing --
3.3.1.FixL --
3.3.2.DevS (DosS) and DosT --
3.3.3.AfGcHK --
3.4.Aerotaxis Control for the Regulation of Bacterial Flagellar Rotation --
3.4.1.HemAT --
3.4.2.Aer2 --
3.5.Synthesis and Hydrolysis of Nucleotide Second Messengers --
3.5.1.YddV (DosC) and EcDOS (DosP) --
3.5.2.HemDGC --
3.5.3.AvGReg and BpeGReg --
3.5.4.AxPDEA1 --
3.5.5.Atypical sGCs: Gyc-88E and GCY-35 --
3.5.6.HemAC-Lm --
3.6.Conclusions --
References --
ch. 4 Haem-based Sensors of Carbon Monoxide / Shigetoshi Aono --
4.1.Introduction --
4.2.Biological Production of CO --
4.2.1.Endogenous CO Production for Ligand of the Metal Clusters in Hydrogenases --
4.2.2.Endogenous CO Production by Haemoxygenases --
4.3.Biological Utilization of CO --
4.3.1.Ni/Fe CO Dehydrogenase Note continued: 4.3.2.Mo/Cu CO Dehydrogenase --
4.4.Bacterial CO-sensor Protein CooA --
4.4.1.Structure of CooA --
4.4.2.Allosteric Control of CRP as a Model of CooA --
4.4.3.Allosteric Control of CooA by CO --
4.4.4.Coordination Structures of the Haem in CooA --
4.4.5.Redox Properties of the Haem in CooA --
4.4.6.Spectroscopic Properties of the Haem in CooA --
4.4.7.Ligand Discrimination of CooA --
4.4.8.CO-binding Kinetics of CooA --
4.4.9.DNA Binding and Transcriptional Activation of CooA --
4.5.Bacterial CO-sensor Protein RcoM --
4.5.1.PAS Domain in RcoM --
4.5.2.Spectroscopic Properties of the PAS Domain in RcoM --
4.5.3.Coordination Structure of the Haem in RcoM --
4.5.4.CO-binding Kinetics of RcoM --
4.5.5.LytTR Domain as a DNA-binding Motif --
4.5.6.DNA Binding of LytTR Domain --
4.6.Mammalian CO-sensor Proteins NPAS2 and CLOCK --
4.6.1.Structure of CLOCK/BMAL1 bHLH-PAS Domains --
4.6.2.DNA Binding of bHLH Domain Note continued: 5.4.6.Corynebacterium glutamicum ArnR --
5.5.Conclusions and Future Perspectives --
Acknowledgements --
References --
ch. 6 Nonhaem Iron-based Sensors of Reactive Oxygen and Nitrogen Species / Dayeon Nam --
6.1.Introduction --
6.2.Sensors for Reactive Oxygen Species --
6.2.1.Transcription Factors that Defend Against ROS --
6.2.2.PerR as Peroxide Sensor --
6.2.3.Redox Sensor SoxR and Reactive Oxygen Species --
6.2.4.Regulator Protein Utilizing Nonhaem Iron and ROS --
6.3.Sensor Proteins for Reactive Nitrogen Species --
6.3.1.Reactive Nitrogen Species in Biological System --
6.3.2.Biological Significance of NO: As a Key Molecule for Biological Signal Transduction and Respiratory Denitrification and as a Potent Oxidizing Cytotoxin to Fight Invading Pathogens --
6.3.3.NorR as NO Sensor --
6.3.4.Iron-Sulfur Proteins as NO Sensors --
6.4.Conclusions --
References --
ch. 7 Mammalian O2 Sensing and Signalling / Michael J. Knapp --
7.1.Cellular O2 Sensing Note continued: 7.1.1.HIF Transcriptional Regulator --
7.1.2.Other O2-sensing Enzymes --
7.1.3.Discovering New Targets for the HIF Hydroxylases --
7.1.4.New Target Identification --
7.1.5.Selected Hypoxia-sensitive Pathways --
7.2.Hydrogen Sulfide and Hypoxia --
7.3.FBXL5 --
7.4.Tissue Signalling --
7.4.1.Acute Hypoxia Sensing by Mammalian Tissue --
7.5.Conclusions --
Acknowledgements --
References --
ch. 8 Plant Ethylene Sensing and Signalling / Brad M. Binder --
8.1.Introduction --
8.2.Overview of Ethylene Biosynthesis --
8.3.Overview of the Ethylene Signal-transduction Pathway in Plants --
8.4.The Ethylene Receptors --
8.4.1.Ethylene-binding Domain --
8.4.2.Copper and Ethylene Binding --
8.4.3.GAF Domain --
8.4.4.Kinase Domain --
8.4.5.Receiver Domain --
8.4.6.Unique and Nonoverlapping Functions of the Ethylene Receptors in Arabidopsis --
8.4.7.Receptor Clusters --
8.4.8.Other Receptor --
Protein Interactions --
8.5.Ethylene Signalling in Nonplants --
8.6.Summary Note continued: Acknowledgements --
References.

✦ Subjects

Cells;Biochemistry;Hemeproteins;chemistry;Gases;chemistry;Iron-Sulfur Proteins;chemistry;Signal Transduction;Ethylenes;chemistry