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Chaperones

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Cover of 'Chaperones'

Table of Contents

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    Book Overview
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    Chapter 1 Targeted Deletion of Hsf1, 2, and 4 Genes in Mice
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    Chapter 2 Role of Heat Shock Factors in Stress-Induced Transcription
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    Chapter 3 Monitoring of the Heat Shock Response with a Real-Time Luciferase Reporter
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    Chapter 4 Quantitative Profiling of Chaperone/Client Interactions with LUMIER Assay
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    Chapter 5 Measurement of Chaperone-Mediated Effects on Polyglutamine Protein Aggregation by the Filter Trap Assay
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    Chapter 6 Fluorescent-Linked Enzyme Chemoproteomic Strategy (FLECS) for Identifying HSP70 Inhibitors
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    Chapter 7 A High-Throughput Screen for Inhibitors of the Hsp90-Chaperone Machine
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    Chapter 8 Primary Colorectal Cells Culture as a Translational Research Model
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    Chapter 9 Cell Death and Survival Assays
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    Chapter 10 Detecting the Potential Pharmacological Synergy of Drug Combination by Viability Assays In Vitro
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    Chapter 11 Proteomic Profiling of Hsp90 Inhibitors
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    Chapter 12 Analysis of HspB1 (Hsp27) Oligomerization and Phosphorylation Patterns and Its Interaction with Specific Client Polypeptides
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    Chapter 13 Nucleotide Exchange Factors for Hsp70 Chaperones
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    Chapter 14 Determination of Hsp90 Activity Through Activation of Glucocorticoid Receptors in Yeast
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    Chapter 15 Bacterial Hsp90 ATPase Assays
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    Chapter 16 Detecting Posttranslational Modifications of Hsp90
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    Chapter 17 Chromatin Immunoprecipitation (ChIP) of Heat Shock Protein 90 (Hsp90)
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    Chapter 18 A Workflow Guide to RNA-seq Analysis of Chaperone Function and Beyond
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    Chapter 19 Computational Modeling of the Hsp90 Interactions with Cochaperones and Small-Molecule Inhibitors
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    Chapter 20 Computational Analysis of the Chaperone Interaction Networks
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    Chapter 21 Immunohistochemistry of Human Hsp60 in Health and Disease: From Autoimmunity to Cancer
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    Chapter 22 Immunohistochemical and Flow Cytometric Analysis of Intracellular and Membrane-Bound Hsp70, as a Putative Biomarker of Glioblastoma Multiforme, Using the cmHsp70.1 Monoclonal Antibody
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    Chapter 23 Detection and Analysis of Extracellular Hsp90 (eHsp90)
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    Chapter 24 Molecular Chaperone Receptors
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    Chapter 25 Creation of Recombinant Chaperone Vaccine Using Large Heat Shock Protein for Antigen-Targeted Cancer Immunotherapy
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    Chapter 26 A Novel Heat Shock Protein 70-based Vaccine Prepared from DC-Tumor Fusion Cells
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    Chapter 27 Hsp70: A Cancer Target Inside and Outside the Cell
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    Chapter 28 Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding
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    Chapter 29 Clinical Evaluation and Biomarker Profiling of Hsp90 Inhibitors
Attention for Chapter 15: Bacterial Hsp90 ATPase Assays
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Chapter title
Bacterial Hsp90 ATPase Assays
Chapter number 15
Book title
Chaperones
Published in
Methods in molecular biology, January 2018
DOI 10.1007/978-1-4939-7477-1_15
Pubmed ID
Book ISBNs
978-1-4939-7476-4, 978-1-4939-7477-1
Authors

Joel R. Hoskins, Sue Wickner, Shannon M. Doyle

Abstract

Bacterial Hsp90 is an ATP-dependent molecular chaperone involved in protein remodeling and activation. The E. coli Hsp90, Hsp90Ec, collaborates in protein remodeling with another ATP-dependent chaperone, DnaK, the E. coli Hsp70. Both Hsp90Ec and DnaK hydrolyze ATP and client (substrate) proteins stimulate the hydrolysis. Additionally, ATP hydrolysis by the combination of Hsp90Ec and DnaK is synergistically stimulated in the presence of client (substrate). Here, we describe two steady-state ATPase assays used to monitor ATP hydrolysis by Hsp90Ec and DnaK as well as the synergistic stimulation of ATP hydrolysis by the combination of Hsp90Ec and DnaK in the presence of a client (substrate). The first assay is a spectrophotometric assay based on enzyme-coupled reactions that utilize the ADP formed during ATP hydrolysis to oxidize NADH. The second assay is a more sensitive method that directly quantifies the radioactive inorganic phosphate released following the hydrolysis of [γ-33P] ATP or [γ-32P] ATP.

Mendeley readers

The data shown below were compiled from readership statistics for 6 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 6 100%

Demographic breakdown

Readers by professional status Count As %
Student > Master 2 33%
Student > Bachelor 1 17%
Researcher 1 17%
Student > Ph. D. Student 1 17%
Unknown 1 17%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 3 50%
Pharmacology, Toxicology and Pharmaceutical Science 1 17%
Agricultural and Biological Sciences 1 17%
Unknown 1 17%