ArticleScientific reports2022
Dimerization processes for light-regulated transcription factor Photozipper visualized by high-speed atomic force microscopy.
Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- High-speed atomic force microscopy and 3D modeling reveal the structural dynamics of ADAR1 complexes.Nature communications · 2025Article
- Multimeric transcription factor BCL11A utilizes two zinc-finger tandem arrays to bind clustered short sequence motifs.Nature communications · 2025Article
- Structural insights into CDF1 accumulation on the CONSTANS promoter via a plant-specific DNA-binding domain.Nature plants · 2025Article
- Membrane tubulation induced by a bacterial glycolipid.Scientific reports · 2025Article
- Spatiotemporal resolution in high-speed atomic force microscopy for studying biological macromolecules in action.Microscopy (Oxford, England) · 2023Review
- A Critical Review on the Sensing, Control, and Manipulation of Single Molecules on Optofluidic Devices.Micromachines · 2022Review
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Authors and funding
4 authors.
Funding
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Abstract
Dimerization is critical for transcription factors (TFs) to bind DNA and regulate a wide variety of cellular functions; however, the molecular mechanisms remain to be completely elucidated. Here, we used high-speed atomic force microscopy (HS-AFM) to observe the dimerization process for a photoresponsive TF Photozipper (PZ), which consists of light-oxygen-voltage-sensing (LOV) and basic-region-leucine-zipper (bZIP) domains. HS-AFM visualized not only the oligomeric states of PZ molecules forming monomers and dimers under controlled dark-light conditions but also the domain structures within each molecule. Successive AFM movies captured the dimerization process for an individual PZ molecule and the monomer-dimer reversible transition during dark-light cycling. Detailed AFM images of domain structures in PZ molecules demonstrated that the bZIP domain entangled under dark conditions was loosened owing to light illumination and fluctuated around the LOV domain. These observations revealed the role of the bZIP domain in the dimerization processes of a TF.
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