Abstract
Heat shock proteins (Hsps) are molecular chaperones that oppose stress-induced denaturation of other proteins. Hsps are present in all organisms. Apart from assisting in the efficient folding of newly synthesized proteins they maintain pre-existing proteins in a stable conformation, preventing their aggregation, under stress conditions. The latter role, essential for thermal adaptation, requires that the chaperone system change from a folding to a storing function at heat shock temperatures. The temperature at which this change occurs depends on the presence of a thermosensor in at least one of the components of the chaperone systems. In this review, we focus on the bacterial GroE and DnaK systems, describe their temperature-sensitive protein components, and the location of the thermosensor within the structure of these components. While the thermosensor of the GroE system is located at the inter-ring interface of GroEL, that of the DnaK system occurs in its co-chaperone GrpE. Analysis of these examples demonstrates the amazing mechanistic diversity of thermal stress adaptation and of functional convergence of structurally unrelated proteins.
Keywords: DnaK, GroEL, GrpE, heat shock protein, protein folding, thermal adaptation
Current Protein & Peptide Science
Title: Thermal Adaptation of Heat Shock Proteins
Volume: 9 Issue: 6
Author(s): A. Muga and F. Moro
Affiliation:
Keywords: DnaK, GroEL, GrpE, heat shock protein, protein folding, thermal adaptation
Abstract: Heat shock proteins (Hsps) are molecular chaperones that oppose stress-induced denaturation of other proteins. Hsps are present in all organisms. Apart from assisting in the efficient folding of newly synthesized proteins they maintain pre-existing proteins in a stable conformation, preventing their aggregation, under stress conditions. The latter role, essential for thermal adaptation, requires that the chaperone system change from a folding to a storing function at heat shock temperatures. The temperature at which this change occurs depends on the presence of a thermosensor in at least one of the components of the chaperone systems. In this review, we focus on the bacterial GroE and DnaK systems, describe their temperature-sensitive protein components, and the location of the thermosensor within the structure of these components. While the thermosensor of the GroE system is located at the inter-ring interface of GroEL, that of the DnaK system occurs in its co-chaperone GrpE. Analysis of these examples demonstrates the amazing mechanistic diversity of thermal stress adaptation and of functional convergence of structurally unrelated proteins.
Export Options
About this article
Cite this article as:
Muga A. and Moro F., Thermal Adaptation of Heat Shock Proteins, Current Protein & Peptide Science 2008; 9 (6) . https://dx.doi.org/10.2174/138920308786733903
DOI https://dx.doi.org/10.2174/138920308786733903 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
Call for Papers in Thematic Issues
Advancements in Proteomic and Peptidomic Approaches in Cancer Immunotherapy: Unveiling the Immune Microenvironment
The scope of this thematic issue centers on the integration of proteomic and peptidomic technologies into the field of cancer immunotherapy, with a particular emphasis on exploring the tumor immune microenvironment. This issue aims to gather contributions that illustrate the application of these advanced methodologies in unveiling the complex interplay ...read more
Artificial Intelligence for Protein Research
Protein research, essential for understanding biological processes and creating therapeutics, faces challenges due to the intricate nature of protein structures and functions. Traditional methods are limited in exploring the vast protein sequence space efficiently. Artificial intelligence (AI) and machine learning (ML) offer promising solutions by improving predictions and speeding up ...read more
Nutrition and Metabolism in Musculoskeletal Diseases
The musculoskeletal system consists mainly of cartilage, bone, muscles, tendons, connective tissue and ligaments. Balanced metabolism is of vital importance for the homeostasis of the musculoskeletal system. A series of musculoskeletal diseases (for example, sarcopenia, osteoporosis) are resulted from the dysregulated metabolism of the musculoskeletal system. Furthermore, metabolic diseases (such ...read more
Protein Folding, Aggregation and Liquid-Liquid Phase Separation
Protein folding, misfolding and aggregation remain one of the main problems of interdisciplinary science not only because many questions are still open, but also because they are important from the point of view of practical application. Protein aggregation and formation of fibrillar structures, for example, is a hallmark of a ...read more
Related Journals
- Author Guidelines
- Graphical Abstracts
- Fabricating and Stating False Information
- Research Misconduct
- Post Publication Discussions and Corrections
- Publishing Ethics and Rectitude
- Increase Visibility of Your Article
- Archiving Policies
- Peer Review Workflow
- Order Your Article Before Print
- Promote Your Article
- Manuscript Transfer Facility
- Editorial Policies
- Allegations from Whistleblowers
Related Articles
-
Drug Disposition in Pathophysiological Conditions
Current Drug Metabolism Fluoride Effects: The Two Faces of Janus
Current Medicinal Chemistry Molecular Determinants of Vascular Calcification: A Bench to Bedside View
Current Molecular Medicine Tissue Engineering in Achilles Tendon Reconstruction; The Role of Stem Cells, Growth Factors and Scaffolds
Current Stem Cell Research & Therapy Atrial Fibrillation: Epidemiology and Peculiarities in the Elderly
Cardiovascular & Hematological Agents in Medicinal Chemistry Novel Drug Targets in Malaria Parasite with Potential to Yield Antimalarial Drugs with Long Useful Therapeutic Lives
Current Pharmaceutical Design Circulating Advanced Oxidation Protein Products as Oxidative Stress Biomarkers and Progression Mediators in Pathological Conditions Related to Inflammation and Immune Dysregulation
Current Medicinal Chemistry Natural Small Molecules as Stabilizers and Activators of Cancer-Associated NQO1 Polymorphisms
Current Drug Targets Castration Resistant Prostate Cancer: From Emerging Molecular Pathways to Targeted Therapeutic Approaches
Clinical Cancer Drugs Pharmacological Properties and Therapeutic Potential of Naringenin: A Citrus Flavonoid of Pharmaceutical Promise
Current Pharmaceutical Design Aneuploidy-Inducing Mutations in Mitotic Checkpoint Protein hMad1-Carboxi Terminal Domain Analyzed by SAR and Computational Mutagenesis
Current Proteomics The Ability of Melatonin to Counteract Lipid Peroxidation in Biological Membranes
Current Molecular Medicine Senescence of the Brain: Focus on Cognitive Kinases
Current Pharmaceutical Design Disruption of Circadian Rhythms and Sleep in Critical Illness and its Impact on the Development of Delirium
Current Pharmaceutical Design Collateral Damage: Contribution of Peripheral Inflammation to Neurodegenerative Diseases
Current Topics in Medicinal Chemistry Hyaluronan and Hyaluronan Synthases: Potential Therapeutic Targets in Cancer
Current Drug Targets - Cardiovascular & Hematological Disorders The Toxicology of Chemokine Inhibition
Mini-Reviews in Medicinal Chemistry Dopamine Receptor Interacting Proteins: Targeting Neuronal Calcium Sensor-1/D2 Dopamine Receptor Interaction for Antipsychotic Drug Development
Current Drug Targets How Satiety Factors Reach CNS Appetite Centers
Immunology, Endocrine & Metabolic Agents in Medicinal Chemistry (Discontinued) Screening and Partial Purification of Cholinesterase Inhibitor from Microalgae
Current Enzyme Inhibition