- Volume
-
pt. A ISBN 9780123738516
Description
Multicellular organisms must be able to adapt to cellular events to accommodate prevailing conditions. Sensory-response circuits operate by making use of a phosphorylation control mechanism known as the "two-component system." Sections include: Computational Analyses of Sequences and Sequence Alignments Biochemical and Genetic Assays of Individual Components of Signaling Systems Physiological Assays and Readouts
Table of Contents
Section I. Computational Analyses of Sequences and Sequence Alignments
CHAPTER 1: Comparative genomic and protein sequence analyses of a complex system controlling bacterial chemotaxis.
CHAPTER 2: Two component systems in microbial communities: Approaches and resources for analyzing metagenomic data sets.
CHAPTER 3: Identification of sensory and signal-transducing domains in two-component signaling systems.
CHAPTER 4: Features of protein-protein interactions in two-component signaling deduced from genomic libraries.
CHAPTER 5: Sporulation phosphorelay proteins and their complexes: Crystallographic characterization.
CHAPTER 6: Control Analysis of Bacterial Chemotaxis Signaling.
CHAPTER 7: Classification of Response Regulators based on their Surface Properties
Section II. Biochemical and Genetic Assays of Individual Components of the Signaling Systems
CHAPTER 8: Purification and Assays of Rhodobacter capsulatus RegB-RegA Two Component Signal Transduction System.
CHAPTER 9: Purification and reconstitution of PYP-phytochrome (Ppr) with biliverdin and 4-hydroxycinnamic acid.
CHAPTER 10: Oxygen and Redox-Sensing by Two-Component Systems That Regulate Behavioral Responses. Behavioral Assays and Structural Studies of Aer using in vivo Disulfide Crosslinking.
CHAPTER 11: Two-Component Signaling in the Virulence of S. aureus: A Silkworm Larvae-Pathogenic Agent Infection Model of Virulence.
CHAPTER 12: TonB System, In vivo Assays and Characterization
CHAPTER 13: Biochemical Characterization of Plant Ethylene Receptors following Transgenic Expression in Yeast.
CHAPTER 14: Structure of SixA, a histidine protein phosphatase of the ArcB HPt domain in E. coli.
CHAPTER 15: Triggering and monitoring light-sensing reactions in protein crystals
CHAPTER 16
CHAPTER 17: Application of Fluorescence Resonance Energy Transfer to Examine EnvZ/OmpR Interactions
CHAPTER 18: Gene promoter scan (GPS) methodology for identifying and classifying co-regulated promoters.
CHAPTER 19: Targeting two-component signal transduction: A novel drug discovery system.
CHAPTER 20: The essential YycFG two-component system of Bacillus subtilis
Section III. Physiological Assays and Readouts
CHAPTER 21: Isolation and Characterization of Chemotaxis Mutants of the Lyme Disease Spirochete Borrelia burgdorferi Using Allelic Exchange Mutagenesis, Flow Cytometry and Cell Tracking.
CHAPTER 22: Phosphorylation assays of chemotaxis two-component system proteins in Borrelia burgdorferi.
CHAPTER 23: Regulation of Respiratory Genes by ResD-ResE Signal Transduction System in Bacillus subtilis.
CHAPTER 24: Physiological and genetic characterization of two-component systems in Myxococcus.
CHAPTER 25: Detection and measurement of two-component systems that control dimorphism and virulence in fungi.
CHAPTER 26: Using Two-Component Systems and other Bacterial Regulatory Factors for the Fabrication of Synthetic Genetic Devices.
- Volume
-
pt. B ISBN 9780123738523
Description
Multicellular organisms must be able to adapt to cellular events to accommodate prevailing conditions. Sensory-response circuits operate by making use of a phosphorylation control mechanism known as the "two-component system."
Sections in Two-Component Signaling Systems, Part B include:
Structural Approaches
Reconstitution of Heterogeneous Systems
Intracellular Methods and Assays
Genome-Wide Analyses of Two-Component Systems
Table of Contents
Section I: Structural Approaches
[1]: The PICM Chemical Scanning Method for Identifying Domain-Domain and Protein-Protein Interfaces: Applications to the Core Signaling Complex of E. coli Chemotaxis
[2]: Use of Site-Directed Cysteine and Disulfide Chemistry to Probe Protein Structure and Dynamics: Applications to Soluble and Transmembrane Receptors of Bacterial Chemotaxis
[3]: Measuring Distances by Pulsed Dipolar ESR Spectroscopy: Spin-Labeled Histidine Kinases
[4]: Rigid Body Refinement of Protein Complexes with Long-Range Distance Restraints from Pulsed Dipolar ESR
[5]: TonB/TolA Amino-Terminal Domain Modeling
[6]: Functional Dynamics of Response Regulators Using NMR Relaxation Techniques
[7]: The Design and Development of Tar-EnvZ Chimeric Receptors
[8]: Functional and Structural Characterization of EnvZ, an Osmosensing Histidine Kinase of E. coli
[9]: Light Modulation of Histidine-Kinase Activity in Bacterial Phytochromes Monitored by Size Exclusion Chromatography, Crosslinking, and Limited Proteolysis
[10]: A Temperature-Sensing Histidine Kinase-Function, Genetics, and Membrane Topology
[11]: The Regulation of Histidine Sensor Kinase Complexes by Quorum Sensing Signal Molecules
Section II: Reconstitution of Heterogeneous Systems
[12]: Liposome-Mediated Assembly of Receptor Signaling Complexes
[13]: Analyzing Transmembrane Chemoreceptors Using In Vivo Disulfide Formation Between Introduced Cysteines
[14]: Using Nanodiscs to Create Water-Soluble Transmembrane Chemoreceptors Inserted in Lipid Bilayers
[15]: Assays for CheC, FliY, and CheX as Representatives of Response Regulator Phosphatases
[16]: Genetic Dissection of Signaling Through the Rcs Phosphorelay
Section III: Intracellular Methods and Assays
[17]: In Vivo Measurement by FRET of Pathway Activity in Bacterial Chemotaxis
[18]: In Vivo and In Vitro Analysis of the Rhodobacter sphaeroides Chemotaxis Signaling Complexes
[19]: In Vivo Crosslinking Methods for Analyzing the Assembly and Architecture of Chemoreceptor Arrays
[20]: A "Bucket of Light" for Viewing Bacterial Colonies in Soft Agar
[21]: Phenotypic Suppression Methods for Analyzing Intra- and Inter-Molecular Signaling Interactions of Chemoreceptors
[22]: Single-Cell Analysis of Gene Expression by Fluorescence Microscopy
Section IV: Genome-Wide Analyses of Two-Component Systems
[23]: Two-Component Systems of Mycobacterium tuberculosis-Structure-Based Approaches
[24]: Transcriptomic Analysis of ArlRS Two-Component Signaling Regulon, a Global Regulator, in Staphylococcus aureus
[25]: Global Analysis of Two-Component Gene Regulation in H. pylori by Mutation Analysis and Transcriptional Profiling
[26]: Phosphotransfer Profiling: Systematic Mapping of Two-Component Signal Transduction Pathways and Phosphorelays
[27]: Identification of Histidine Phosphorylations in Proteins Using Mass Spectrometry and Affinity-Based Techniques
Subject Index
Author Index
- Volume
-
pt. C ISBN 9780123813473
Description
Multicellular organisms must be able to adapt to cellular events to accommodate prevailing conditions. Sensory-response circuits operate by making use of a phosphorylation control mechanism known as the "two-component system." This volume, the third in a three-volume treatment edited by the same group of editors, includes a wide range of methods, including those dealing with the Sln-1 kinase pathway, triazole sensitivity in C. albicans, and histidine kinases in cyanobacteria circadian clock.
Table of Contents
Characterizing cross-talk in vivo: avoiding pitfalls and over-interpretation Albert Siryaporn and Mark Goulian
Inference of Direct Residue Contacts in Two-Component Signaling Bryan Lunt, Hendrik Szurmant, Andrea Procaccini, James A. Hoch, Terence Hwa and Martin Weigt
Computational Modeling of Phosphotransfer Complexes in Two-Component Signaling Alexander Schug, Martin Weigt, James A. Hoch, Jose N. Onuchic, Terence Hwa, Hendrik Szurmant
Kinetic studies of the yeast His-Asp phosphorelay signaling pathway Alla O. Kaserer, Babak Andi, Paul F. Cook and Ann H. West
Purification of MBP-EnvZ fusion proteins using an automated system Ricardo Oropeza and Edmundo Calva
Measurement of Response Regulator Autodephosphorylation Rates Spanning Six Orders of Magnitude Robert B. Bourret, Stephanie A. Thomas, Stephani C. Page, Rachel L. Creager-Allen, Aaron M. Moore, and Ruth E. Silversmith
Transmembrane receptors chimeras to probe Hamp domain function Jurgen U. Linder and Joachim E. Schultz
Light-Activated Bacterial LOV-domain Histidine Kinases Tong-Seung Tseng, Marcus A. Frederickson, Winslow R. Briggs and Roberto A. Bogomolni
Characterization of Bacteriophytochromes from Photosynthetic Bacteria: Histidine Kinase Signaling Triggered by light and redox sensing Eric Giraud, Jerome Lavergne and Andre Vermeglio
Biophysical assays for protein interactions in the Wsp sensory system and biofilm formation Nabanita De, Marcos V.A.S. Navarro, Qi Wang, Petya V. Krasteva and Holger Sondermann
High throughput screening of bacterial protein localization John N. Werner and Zemer Gitai
In vitro and in vivo analysis of the ArcB/A redox signaling pathway Adrian F. Alvarez and Dimitris Georgellis
Potassium sensing histidine kinase in Bacillus subtilis Daniel Lopez, Erin Gontang and Roberto Kolter
Two Component Systems and Regulation of Developmental Progression in Myxococcus Xanthus Bongsoo Lee, Andreas Schramm, and Penelope I. Higgs
Two-component signaling to the stress MAP kinase cascade in fission yeast Susumu Morigasaki and Kazuhiro Shiozaki
Genetic and Biochemical Analysis of the SLN1 Pathway in Saccharomyces cerevisiae Jan S. Fassler
Analysis of mitogen-activated protein kinase phosphorylation in response to stimulation of histidine kinase signaling pathways in Neurospora Carol A. Jones and Katherine A. Borkovich
Biochemical Characterization of Plant Hormone Cytokinin Receptor Histidine Kinases Using Microorganisms Takeshi Mizuno and Takafumi Yamashino
Characterization of Pseudo-Response Regulators In Plants Woe-Yeon Kim, Patrice A. Salome, Sumire Fujiwara, David E. Somers and C. Robertson McClung
Reversible Histidine Phosphorylation in Mammalian Cells: A Teeter-Totter Formed by Nucleoside Diphosphate Kinase and Protein Histidine Phosphatase Thomas Wieland, Hans-Joerg Hippe, Katrin Ludwig, Xiao-Bo Zhou, Michael Korth and Susanne Klumpp
Histidine phosphorylation in histones and in other mammalian proteins Paul G. Besant and P.V. Attwood
by "Nielsen BookData"
