Gas Sensing in Cells
eBook - ePub

Gas Sensing in Cells

  1. 303 pages
  2. English
  3. ePUB (mobile friendly)
  4. Available on iOS & Android
eBook - ePub

Gas Sensing in Cells

About this book

Gas molecules such as O 2, NO, CO and ethylene are present in the environment and are endogenously (enzymatically) produced to act as signalling molecules in biological systems, including the regulation of metabolic networks, chemotaxis, circadian rhythms, mammalian hypoxia responses, and plant ethylene responses by transcriptional, translational, or post translational control. Sensing these gas molecules is the first step in their acting as signalling molecules. When a sensor domain/protein senses an external signal, intra- and inter-molecular signal transductions take place to regulate the biological function of a regulatory domain/protein such as DNA-binding, enzymatic activity, or protein–protein interaction. Interaction between gas molecules and sensor proteins is essential for recognition of gas molecules. Metal-containing prosthetic groups such as haem, iron–sulfur clusters, and non-haem iron centres are widely used. As these metal-containing centres are good spectroscopic probes, detail characterizations have utilized spectroscopic techniques along with X-ray crystallography.
Covering both the signalling and sensing of gaseous molecules, this book provides the first comprehensive overview of gas sensor proteins in both prokaryotic and eukaryotic cells. This book will be particularly interesting to postgraduates and researchers in biochemistry, molecular biology and metallobiology.

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Yes, you can access Gas Sensing in Cells by Shigetoshi Aono in PDF and/or ePUB format, as well as other popular books in Physical Sciences & Biochemistry. We have over one million books available in our catalogue for you to explore.

Information

CHAPTER 1
Overview of Gas-sensing Systems
Shigetoshi Aono
a Institute for Molecular Science, 5-1 Higashiyama, Myodaiji, Okazaki 444-8787, Japan;
b Okazaki Institute for Integrative Bioscience, 5-1 Higashiyama, Myodaiji, Okazaki 444-8787, Japan

1.1 Introduction

Gas molecules such as O2, NO, CO and ethylene are present in the environment and are endogenously (enzymatically) produced to act as signalling molecules in biological systems. Sensing these gas molecules is the first step in their acting as signalling molecules. Sensor proteins are usually required. Input signals generated by gas sensing have to transduce to output signals that regulate biological functions. This is achieved by biological signal-transduction systems, as described in Section 1.2.
Recognition of the cognate gas molecules is a general mechanism of functional regulation for gas-sensor proteins. This induces conformational changes in proteins that controls their activities for following signal transductions. Interaction between gas molecules and sensor proteins is essential for recognition of gas molecules. Metal-containing prosthetic groups are widely used. It is known that O2, NO, and reactive oxygen/nitrogen species react with thiol groups and nucleotides to induce biological signal transductions.1–101-10 However, this book will focus on metal-containing gas-sensor proteins and the signalling systems working with them. The sensor proteins discussed here are summarized in Table 1.1. The basic properties of typical prosthetic groups used by these proteins are summarized in Section 1.3. Chapters 2, 3, and 4 will cover the haem-based NO, O2, and CO sensors, respectively. Iron–sulfur cluster-based sensors will be addressed in Chapter 5, followed by Chapter 6 describing nonhaem iron-based sensors. The book also will cover mammalian O2 signalling systems and plants ethylene signalling systems in Chapters 7 and 8, respectively.
Table 1.1 Sensor proteins discussed in this book.
Sensor protein Organism Sensor domaina Prosthetic groupb Effector Functionc Chapter
sGC Mammals H-NOX Haem NO GC 2
H-NOX Clostridium botulinum, Caldanaerobacter subterraneus, Legionella pneumophila, Nostoc sp., Pseudoalteromonas atlantica, Shewanella oneidensis H-NOX Haem NO/O2 Standalone or fused to regulatory domains 2
Shewanella woodyi, Vibrio cholerae
YybT Bacillus subtilis, Geobacillus thermodenitrificans PAS Haem NO/haem PDE 2
E75 Bombyx mori, Drosophila melanogaster, Oncopeltus fasciatus Nuclear receptor ligand-binding domain Haem NO TR 2
NosP Pseudomonas aeruginosa FIST Haem NO HK in TCS 2
DNR Pseudomonas aeruginosa CRP/FNR Haem NO TR 2
FixL Bradyrhizobium japonicum, Sinorhizobium meliloti PAS Haem O2 HK in TCS 3
DevS (DosS) Mycobacterium tuberculosis GAF Haem O2/redox change HK in TCS 3
DosT Mycobacterium tuberculosis GAF Haem O2 HK in TCS 3
AfGcHK Anaeromyxobacter sp. GCS Haem O2 HK in TCS 3
Aer Escherichia coli PAS FMN Change(s) in redox potential, H+ motive force, or electron flux MCP 3
Aer2 Pseudomonas aeruginosa PAS Haem O2 MCP 3
HemAT Bacillus subtilis, Halobactrium salinarum GCS Haem O2 MCP 3
YddV (DosC) Escherichia coli GCS Haem O2 DGC 3
EcDOS (DosP) Escherichia coli PAS Haem O2 PDE 3
HemDGC Desulfotalea psychrophila GCS Haem O2 DGC 3
AvGReg Azotobacter vinelandii GCS Haem O2 DGC 3
BpeGReg Bordetella pertussis GCS Haem O2 DGC 3
AxPDEA1 Gluconacetobacter xylinus PAS Haem O2 PDE 3
Gyc-89 Da Drosophila melanogaster H-NOX Haem O2 GC 3
Gyc-89Db
Gyc-88E
GCY-35 Caenorhabditis elegans H-NOX Haem O2 GC 3
HemAC-Lm Leishmania major GCS Haem O2 AC 3
CooA Carboxydothermus hydrogenoformans, Rhodospirillum rubrum CRP/FNR Haem CO TR 4
RcoM Burkholderia xenovorans PAS Haem CO TR 4
NPAS2 Mammals PAS Haem CO TR 4
CLOCK Mammals PAS Haem CO TR 4
CBS Mammals - Haem CO/NO CBS 4
FNR Escherichia coli, Aliivibrio fischeri CRP/FNR [4Fe–4S] O2 TR 5
FNR Bacillus subtilis CRP/FNR [4Fe–4S] O2 TR 5
FnrP Paracoccus denitrificans CRP/FNR [4Fe–4S] O2 TR 5
ANR Pseudomonas putida CRP/FNR [4Fe–4S] O2 TR 5
NreB Staphylococci PAS [4Fe–4S] O2 HK in TCS 5
AirS Staphylococcus aureus GAF [2Fe–2S] O2 HK in TCS 5
SoxR Escherichia coli MerR [2Fe–2S] O2, redox-active compounds TR 5, 6
IscR Escherichia coli Rrf2 [2Fe–2S] O2/oxidative stress TR 5
RsrR Streptomyces venezuelae Rrf2 [2Fe–2S] O2? TR 5
NsrR Bacillus subtilis, Streptomyces coelicolor Rrf2 [4Fe–4S] NO TR 5, 6
WhiB-like (Wbl) proteins Actinobacteria ? [4Fe–4S] NO/O2/redox stress...

Table of contents

  1. Cover
  2. Title
  3. Copyright
  4. Contents
  5. Chapter 1 Overview of Gas-sensing Systems
  6. Chapter 2 Haem-based Sensors of Nitric Oxide
  7. Chapter 3 Haem-based Sensors of Dioxygen
  8. Chapter 4 Haem-based Sensors of Carbon Monoxide
  9. Chapter 5 Iron–Sulfur Cluster-based Sensors
  10. Chapter 6 Nonhaem Iron-based Sensors of Reactive Oxygen and Nitrogen Species
  11. Chapter 7 Mammalian O2 Sensing and Signalling
  12. Chapter 8 Plant Ethylene Sensing and Signalling
  13. Subject Index