title: In situ assembly of macromolecular complexes triggered by light.
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.
authors.affiliation: Institute of Biochemistry, Biocenter, Goethe-University Frankfurt, Max-von-Laue-Strasse 9, D-60438 Frankfurt/M., Germany.
authors.forename: Christian
authors.initials: C
authors.lastname: Grunwald
authors.forename: Katrin
authors.initials: K
authors.lastname: Schulze
authors.forename: Annett
authors.initials: A
authors.lastname: Reichel
authors.forename: Victor U
authors.initials: VU
authors.lastname: Weiss
authors.forename: Dieter
authors.initials: D
authors.lastname: Blaas
authors.forename: Jacob
authors.initials: J
authors.lastname: Piehler
authors.forename: Karl-Heinz
authors.initials: KH
authors.lastname: Wiesmüller
authors.forename: Robert
authors.initials: R
authors.lastname: Tampé
mesh_terms: D002614:Chelating Agents / Q000737:chemistry; D002850:Chromatography, Gel; D006639:Histidine / Q000737:chemistry; D008027:Light; D058619:Maltose-Binding Proteins; D015394:Molecular Structure; D009571:Nitrilotriacetic Acid / Q000737:chemistry; D009842:Oligopeptides / Q000737:chemistry; D033902:Periplasmic Binding Proteins / Q000737:chemistry* / Q000302:isolation & purification; D011485:Protein Binding; D011487:Protein Conformation; D011973:Receptors, LDL / Q000737:chemistry* / Q000378:metabolism; D011991:Receptors, Virus / Q000737:chemistry* / Q000378:metabolism; D012229:Rhinovirus / Q000737:chemistry / Q000378:metabolism / Q000528:radiation effects; D014771:Virion / Q000378:metabolism / Q000528:radiation effects
chemical_list: D002614:Chelating Agents; D058619:Maltose-Binding Proteins; D009842:Oligopeptides; D033902:Periplasmic Binding Proteins; D011973:Receptors, LDL; D011991:Receptors, Virus; C036053:VLDL receptor; D006639:Histidine; D009571:Nitrilotriacetic Acid