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Journal Article

Fine‐Tuning Protein Self‐Organization by Orthogonal Chemo‐Optogenetic Tools

MPS-Authors
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Jia,  Haiyang
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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Ramirez-Diaz,  Diego A.
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons15815

Schwille,  Petra
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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Fulltext (public)

anie.202008691.pdf
(Publisher version), 6MB

Supplementary Material (public)

anie202008691-sup-0001-misc_information.pdf
(Supplementary material), 541KB

anie202008691-sup-0001-movie_s1.avi
(Supplementary material), 10MB

anie202008691-sup-0001-movie_s2.avi
(Supplementary material), 11MB

anie202008691-sup-0001-movie_s3.avi
(Supplementary material), 11MB

Citation

Sun, H., Jia, H., Ramirez-Diaz, D. A., Budisa, N., & Schwille, P. (2021). Fine‐Tuning Protein Self‐Organization by Orthogonal Chemo‐Optogenetic Tools. Angewandte Chemie International Edition. doi:10.1002/anie.202008691.


Cite as: http://hdl.handle.net/21.11116/0000-0007-D5B6-B
Abstract
A universal gain-of-function approach for the spatiotemporal control of protein activity is highly desirable when reconstituting biological modules in vitro. Here we used orthogonal translation with a photocaged amino acid to map and elucidate molecular mechanisms in the self-organization of the prokaryotic filamentous cell-division protein (FtsZ) that is highly relevant for the assembly of the division ring in bacteria. We masked a tyrosine residue of FtsZ by site-specific incorporation of a photocaged tyrosine analogue. While the mutant still shows self-assembly into filaments, dynamic self-organization into ring patterns can no longer be observed. UV-mediated uncaging revealed that tyrosine 222 is essential for the regulation of the protein's GTPase activity, self-organization, and treadmilling dynamics. Thus, the light-mediated assembly of functional protein modules appears to be a promising minimal-regulation strategy for building up molecular complexity towards a minimal cell.