ArticleProceedings of the National Academy of Sciences of the United States of America2006
Single-molecule detection of structural changes during Per-Arnt-Sim (PAS) domain activation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- A novel fracture lattice in spiny mouse skin facilitates tissue autotomy and regeneration.bioRxiv : the preprint server for biology · 2026Article
- Functional insights into the photoactive yellow protein family from homologs, multidomain proteins, and inferredJournal of bacteriology · 2026Review
- Dynamic rigidity changes enable rapid cell migration on soft substrates.Nature communications · 2025Article
- Reconstruction of ARNT PAS-B Unfolding Pathways by Steered Molecular Dynamics and Artificial Neural Networks.Journal of chemical theory and computation · 2021Article
- Blue light-induced low mechanical stability of ruthenium-based coordination bonds: an AFM-based single-molecule force spectroscopy study.RSC advances · 2020Article
- Combining protein sequence, structure, and dynamics: A novel approach for functional evolution analysis of PAS domain superfamily.Protein science : a publication of the Protein Society · 2018Article
- Investigations of the CLOCK and BMAL1 Proteins Binding to DNA: A Molecular Dynamics Simulation Study.PloS one · 2016Article
- Mechanism of amyloid β-protein dimerization determined using single-molecule AFM force spectroscopy.Scientific reports · 2013Article
- Structure and proposed mechanism for the pH-sensing Helicobacter pylori chemoreceptor TlpB.Structure (London, England : 1993) · 2012Article
- Single-molecule experiments reveal the flexibility of a Per-ARNT-Sim domain and the kinetic partitioning in the unfolding pathway under force.Biophysical journal · 2012Article
- Robustness and evolvability in the functional anatomy of a PER-ARNT-SIM (PAS) domain.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Modulating native-like residual structure in the fully denatured state of photoactive yellow protein affects its refolding.The Journal of biological chemistry · 2010Article
- ARNT PAS-B has a fragile native state structure with an alternative beta-sheet register nearby in sequence space.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Proline 54 trans-cis isomerization is responsible for the kinetic partitioning at the last-step photocycle of photoactive yellow protein.Protein science : a publication of the Protein Society · 2008Article
- PAS-mediated dimerization of soluble guanylyl cyclase revealed by signal transduction histidine kinase domain crystal structure.The Journal of biological chemistry · 2008Article
- Axis-dependent anisotropy in protein unfolding from integrated nonequilibrium single-molecule experiments, analysis, and simulation.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Single-molecule force spectroscopy reveals a mechanically stable protein fold and the rational tuning of its mechanical stability.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
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Authors and funding
6 authors.
Funding
Abstract
The Per-Arnt-Sim (PAS) domain is a ubiquitous protein module with a common three-dimensional fold involved in a wide range of regulatory and sensory functions in all domains of life. The activation of these functions is thought to involve partial unfolding of N- or C-terminal helices attached to the PAS domain. Here we use atomic force microscopy to probe receptor activation in single molecules of photoactive yellow protein (PYP), a prototype of the PAS domain family. Mechanical unfolding of Cys-linked PYP multimers in the presence and absence of illumination reveals that, in contrast to previous studies, the PAS domain itself is extended by approximately 3 nm (at the 10-pN detection limit of the measurement) and destabilized by approximately 30% in the light-activated state of PYP. Comparative measurements and steered molecular dynamics simulations of two double-Cys PYP mutants that probe different regions of the PAS domain quantify the anisotropy in stability and changes in local structure, thereby demonstrating the partial unfolding of their PAS domain upon activation. These results establish a generally applicable single-molecule approach for mapping functional conformational changes to selected regions of a protein. In addition, the results have profound implications for the molecular mechanism of PAS domain activation and indicate that stimulus-induced partial protein unfolding can be used as a signaling mechanism.
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