In situ assembly of macromolecular complexes triggered by light
DC Element | Wert | Sprache |
---|---|---|
dc.contributor.author | Grunwald, Christian | |
dc.contributor.author | Schulze, Katrin | |
dc.contributor.author | Reichel, Annett | |
dc.contributor.author | Weiss, Victor U. | |
dc.contributor.author | Blaas, Dieter | |
dc.contributor.author | Piehler, Jacob | |
dc.contributor.author | Wiesmueller, Karl-Heinz | |
dc.contributor.author | Tampe, Robert | |
dc.date.accessioned | 2021-12-23T16:20:44Z | - |
dc.date.available | 2021-12-23T16:20:44Z | - |
dc.date.issued | 2010 | |
dc.identifier.issn | 00278424 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/13576 | - |
dc.description.abstract | Chemical biology aims for a perfect control of protein complexes in time and space by their site-specific labeling, manipulation, and structured organization. Here we developed a self-inactivated, lock-and-key recognition element whose binding to His-tagged proteins can be triggered by light from zero to nanomolar affinity. Activation is achieved by photocleavage of a tethered intramolecular ligand arming a multivalent chelator head for high-affinity protein interaction. We demonstrate site-specific, stable, and reversible binding in solution as well as at interfaces controlled by light with high temporal and spatial resolution. Multiplexed organization of protein complexes is realized by an iterative in situ writing and binding process via laser scanning microscopy. This light-triggered molecular recognition should allow for a spatiotemporal control of protein-protein interactions and cellular processes by light-triggered protein clustering. | |
dc.description.sponsorship | Bundesministerium fur Bildung und ForschungFederal Ministry of Education & Research (BMBF) [0312031, 0312034]; Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [Ta157/6]; Austrian Science Foundation (FWF)Austrian Science Fund (FWF); We thank Gerhard Spatz-Kumbel for technical assistance and Helge Grossmann for helpful discussions. The work was supported by the Bundesministerium fur Bildung und Forschung (BMBF, Nanobiotechnology 0312031 and 0312034), the Deutsche Forschungsgemeinschaft (DFG, Ta157/6), and the Austrian Science Foundation (FWF). | |
dc.language.iso | en | |
dc.publisher | NATL ACAD SCIENCES | |
dc.relation.ispartof | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | |
dc.subject | biofunctionalized interface | |
dc.subject | FLUORESCENT | |
dc.subject | IMMOBILIZATION | |
dc.subject | light-triggerd chemical biology | |
dc.subject | molecular recognition | |
dc.subject | Multidisciplinary Sciences | |
dc.subject | PROBES | |
dc.subject | protein interaction | |
dc.subject | PROTEINS | |
dc.subject | Science & Technology - Other Topics | |
dc.subject | self-assembly by light | |
dc.subject | SURFACES | |
dc.title | In situ assembly of macromolecular complexes triggered by light | |
dc.type | journal article | |
dc.identifier.doi | 10.1073/pnas.0912617107 | |
dc.identifier.isi | ISI:000276374400007 | |
dc.description.volume | 107 | |
dc.description.issue | 14 | |
dc.description.startpage | 6146 | |
dc.description.endpage | 6151 | |
dc.contributor.orcid | 0000-0002-0403-2160 | |
dc.contributor.orcid | 0000-0002-0056-6819 | |
dc.contributor.researcherid | H-2953-2015 | |
dc.publisher.place | 2101 CONSTITUTION AVE NW, WASHINGTON, DC 20418 USA | |
dcterms.isPartOf.abbreviation | Proc. Natl. Acad. Sci. U. S. A. | |
dcterms.oaStatus | Green Published, Bronze | |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.orcid | 0000-0002-2143-2270 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | PiJa938 | - |
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