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  Mass-sensitive particle tracking to elucidate the membrane-associated MinDE reaction cycle

Heermann, T., Steiert, F., Ramm, B., Hundt, N., & Schwille, P. (2021). Mass-sensitive particle tracking to elucidate the membrane-associated MinDE reaction cycle. Nature Methods, 18(10), 1239-1246. doi:10.1038/s41592-021-01260-x.

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s41592-021-01260-x.pdf (Publisher version), 5MB
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Open access funding provided by Max Planck Society.

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 Creators:
Heermann, Tamara1, Author              
Steiert, Frederik1, Author              
Ramm, Beatrice1, Author              
Hundt, Nikolas2, Author
Schwille, Petra1, Author              
Affiliations:
1Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565169              
2external, ou_persistent22              

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Free keywords: KERNEL DENSITY-ESTIMATION; TO-POLE OSCILLATION; CELL-DIVISION; LABEL-FREE; OPTICAL-DETECTION; ESCHERICHIA-COLI; SINGLE; BINDING; ATP; DYNAMICSBiochemistry & Molecular Biology;
 Abstract: An iSCAT image processing and analysis strategy enables mass-sensitive particle tracking (MSPT) of single unlabeled biomolecules on a supported lipid bilayer. MSPT was used to observe the (dis-)assembly of membrane complexes in real-time. In spite of their great importance in biology, methods providing access to spontaneous molecular interactions with and on biological membranes have been sparse. The recent advent of mass photometry to quantify mass distributions of unlabeled biomolecules landing on surfaces raised hopes that this approach could be transferred to membranes. Here, by introducing a new interferometric scattering (iSCAT) image processing and analysis strategy adapted to diffusing particles, we enable mass-sensitive particle tracking (MSPT) of single unlabeled biomolecules on a supported lipid bilayer. We applied this approach to the highly nonlinear reaction cycles underlying MinDE protein self-organization. MSPT allowed us to determine the stoichiometry and turnover of individual membrane-bound MinD/MinDE protein complexes and to quantify their size-dependent diffusion. This study demonstrates the potential of MSPT to enhance our quantitative understanding of membrane-associated biological systems.

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Language(s): eng - English
 Dates: 2021
 Publication Status: Published in print
 Pages: 13
 Publishing info: -
 Table of Contents: We thank D. Bollschweiler (Cryo-EM MPIB Core Facility) for the initial introduction to the commercial Refeyn OneMP mass photometer, the MPIB Biochemistry Core Facility (Recombinant Protein Production).
 Rev. Type: Peer
 Degree: -

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Project name : project ID 201269156-SFB 1032 (A09)
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Funding organization : Deutsche Forschungsgemeinschaft
Project name : project no. 269423233-TRR 174
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Funding organization : Deutsche Forschungsgemeinschaft

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Title: Nature Methods
  Other : Nature Methods
Source Genre: Journal
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Publ. Info: New York, NY : Nature Pub. Group
Pages: - Volume / Issue: 18 (10) Sequence Number: - Start / End Page: 1239 - 1246 Identifier: ISSN: 1548-7091
CoNE: https://pure.mpg.de/cone/journals/resource/111088195279556