Ultrafast tracking reveals the function of structural domains of single proteins

0518841 - ÚFE 2020 DE eng A - Abstrakt
Holanová, Kristýna - Bujak, Lukasz - Marín, Antonio García - Henrichs, V - Braun, Marcus - Lánský, Zdeněk - Piliarik, Marek
Ultrafast tracking reveals the function of structural domains of single proteins.
European Biophysics Journal With Biophysics Letters. Roč. 48, Supplement: 1 (2019), S92-S92. ISSN 0175-7571. E-ISSN 1432-1017.
[Joint 12th EBSA European Biophysics Congress / 10th IUPAP International Conference on Biological Physics (ICBP). 20.07.2019-24.07.2019, Madrid]
Institucionální podpora: RVO:67985882 ; RVO:86652036
Obor OECD: Biophysics; Biophysics (BTO-N)

Protein-protein interactions and their dynamics have been extensively studied mostly by fluorescence. Fluorescent labels are usually incorporated to discriminate biological processes under study from the complex background or visualize small molecules. To overcome spatio-temporal limitations of fluorescence [1], we employ interferometric detection of scattering (iSCAT). iSCAT detects the light scattered on a protein molecule or a scattering label via its interference with a reference wave, e.g. light partially reflected at a glass coverslip. By these means, it is possible to image very small scattering labels [2] or even unlabeled proteins [3]. PRC1 (protein regulator of cytokinesis 1) belongs to the Ase1/MAP65/PRC1 family of microtubule-associated proteins (MAPs) and plays an important role in cytokinesis. These proteins serve as rigid connections between MTs and can interact with other proteins. Each structural domain of the PRC1 protein seems to play its role but details remain unclear [4]. We studied two different domains via a specific attachment of scattering labels. 3D maps of PRC1 on a single microtubule were measured and analyzed. We observe that each domain has a different behavior and we propose a new functional model of the interaction
Trvalý link: http://hdl.handle.net/11104/0303871