Coupling between global dynamics and signal transduction pathways: a mechanism of allostery for chaperonin GroEL
Abstract
Despite significant efforts toward understanding the molecular basis of allosteric communication, the mechanisms by which local energetic and conformational changes cooperatively diffuse from ligand-binding sites to distal regions across the 3-dimensional structure of allosteric proteins remain to be established. Recent experimental and theoretical evidence supports the view that allosteric communication is facilitated by the intrinsic ability of the biomolecules to undergo collective changes in structure, triggered by ligand binding. Two groups of studies recently proved to provide insights into such intrinsic, structure-induced effects: elastic network models that permit us to visualize the cooperative changes in conformation that are most readily accessible near native state conditions, and information-theoretic approaches that elucidate the most efficient pathways of signal transmission favored by the overall architecture. Using a combination of these two approaches, we highlight, by way of application to the bacterial chaperonin complex GroEL-GroES, how the most cooperative modes of motion play a role in mediating the propagation of allosteric signals. A functional coupling between the global dynamics sampled under equilibrium conditions and the signal transduction pathways inherently favored by network topology appears to control allosteric effects.
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Hiroshi Sugiyama's group has recently developed a new class of artificial TF mimics chemicals based on pyrrole-imidazole polyamides that can target specific DNA sequences and regulate gene expression.
“For example, Hiroshi Sugiyama’s group has recently developed a new class of artificial TF mimics chemicals based on pyrrole-imidazole polyamides that can target specific DNA sequences and regulate gene expression.470”
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Self-citation
- Authors
- Chennubhotla, C., Yang, Z., & Bahar, I.
- Affiliations
- University of Pittsburgh (US)
- Department of Computational Biology, School of Medicine, University of Pittsburgh a , Suite 3064 Biomedical Science Tower 3 3501 Fifth Ave., Pittsburgh, PA 15213, USA bahar@ccbb.pitt.edu +1 (412) 648-3163 +1 (412) 648-3332
- Venue
- Molecular BioSystems
- Publisher
- Oxford University Press (OUP)
- Published
- 2008-02-20
- Volume
- 4
- Issue
- 4
- Pages
- 287-292
- ISSN
- 1742-2051 (ISSN-L)
- 1742-206X
- OpenAlex
- W1972964958
- Cited by
- 102
- References
- 50
- Citations by year
- 2025: 2 · 2024: 1 · 2023: 4 · 2022: 2 · 2021: 1 · 2020: 9 · 2019: 7 · 2018: 1 · 2017: 9 · 2016: 4 · 2015: 3 · 2014: 8 · 2013: 10 · 2012: 7
- FWCI
- 4.52
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Molecular BioSystems (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r33gm068400-03)
- National Institute of General Medical Sciences (#R33 GM068400)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- allosteric communication, signaling pathways, elastic network model, information theory, cooperative conformational change, global dynamics, network topology, protein conformational dynamics
- MeSH terms
- Allosteric Regulation, Computer Simulation, Markov Chains, Models, Chemical, Models, Molecular, Protein Conformation, Signal Transduction, Chaperonin 60
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