Gräter, Frauke

[["dc.bibliographiccitation.firstpage","13385"],["dc.bibliographiccitation.issue","36"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","13390"],["dc.bibliographiccitation.volume","105"],["dc.contributor.author","Puchner, Elias M"],["dc.contributor.author","Alexandrovich, Alexander"],["dc.contributor.author","Kho, Ay Lin"],["dc.contributor.author","Hensen, Ulf"],["dc.contributor.author","Schäfer, Lars V."],["dc.contributor.author","Brandmeier, Birgit"],["dc.contributor.author","Gräter, Frauke"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Gaub, Hermann"],["dc.contributor.author","Gautel, Mathias"],["dc.date.accessioned","2018-02-13T13:12:50Z"],["dc.date.available","2018-02-13T13:12:50Z"],["dc.date.issued","2008-09-09"],["dc.description.abstract","Biological responses to mechanical stress require strain-sensing molecules, whose mechanically induced conformational changes are relayed to signaling cascades mediating changes in cell and tissue properties. In vertebrate muscle, the giant elastic protein titin is involved in strain sensing via its C-terminal kinase domain (TK) at the sarcomeric M-band and contributes to the adaptation of muscle in response to changes in mechanical strain. TK is regulated in a unique dual autoinhibition mechanism by a C-terminal regulatory tail, blocking the ATP binding site, and tyrosine autoinhibition of the catalytic base. For access to the ATP binding site and phosphorylation of the autoinhibitory tyrosine, the C-terminal autoinhibitory tail needs to be removed. Here, we use AFM-based single-molecule force spectroscopy, molecular dynamics simulations, and enzymatics to study the conformational changes during strain-induced activation of human TK. We show that mechanical strain activates ATP binding before unfolding of the structural titin domains, and that TK can thus act as a biological force sensor. Furthermore, we identify the steps in which the autoinhibition of TK is mechanically relieved at low forces, leading to binding of the cosubstrate ATP and priming the enzyme for subsequent autophosphorylation and substrate turnover."],["dc.identifier.doi","10.1073/pnas.0805034105"],["dc.identifier.pmid","18765796"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/12229"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1091-6490"],["dc.relation.haserratum","/handle/2/80234"],["dc.title","Mechanoenzymatics of titin kinase"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","13070"],["dc.bibliographiccitation.issue","37"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","13074"],["dc.bibliographiccitation.volume","102"],["dc.contributor.author","Andresen, Martin"],["dc.contributor.author","Wahl, Markus C."],["dc.contributor.author","Stiel, André C."],["dc.contributor.author","Gräter, Frauke"],["dc.contributor.author","Schäfer, Lars V."],["dc.contributor.author","Trowitzsch, Simon"],["dc.contributor.author","Weber, Gert"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Hell, Stefan W."],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2017-09-07T11:54:19Z"],["dc.date.available","2017-09-07T11:54:19Z"],["dc.date.issued","2005"],["dc.description.abstract","Proteins that can be reversibly photoswitched between a fluorescent and a nonfluorescent state bear enormous potential in diverse fields, such as data storage, in vivo protein tracking, and subdiffraction resolution light microscopy. However, these proteins could hitherto not live up to their full potential because the molecular switching mechanism is not resolved. Here, we clarify the molecular photoswitching mechanism of asFP595, a green fluorescent protein (GFP)-like protein that can be transferred from a nonfluorescent \"off\" to a fluorescent \"on\" state and back again, by green and blue light, respectively. To this end, we establish reversible photoswitching of fluorescence in whole protein crystals and show that the switching kinetics in the crystal is identical with that in solution. Subsequent x-ray analysis demonstrated that upon the absorption of a green photon, the chromophore isomerizes from a trans (off) to a cis (on) state. Molecular dynamics calculations suggest that isomerization occurs through a bottom hula twist mechanism with concomitant rotation of both bonds of the chromophoric methine ring bridge. This insight into the switching mechanism should facilitate the targeted design of photo-switchable proteins. Reversible photoswitching of the protein chromophore system within intact crystals also constitutes a step toward the use of fluorescent proteins in three-dimensional data recording."],["dc.identifier.doi","10.1073/pnas.0502772102"],["dc.identifier.gro","3143804"],["dc.identifier.isi","000231916300014"],["dc.identifier.pmid","16135569"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1359"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0027-8424"],["dc.title","Structure and mechanism of the reversible photoswitch of a fluorescent protein"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","MPIbpc news"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Andresen, Martin"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Wahl, Markus C."],["dc.contributor.author","Hell, Stefan W."],["dc.contributor.author","Stiel, André C."],["dc.contributor.author","Gräter, Frauke"],["dc.contributor.author","Trowitzsch, Simon"],["dc.contributor.author","Schäfer, Lars V."],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Weber, Gert"],["dc.contributor.author","Grubmüller, Helmut"],["dc.date.accessioned","2018-04-23T08:45:37Z"],["dc.date.available","2018-04-23T08:45:37Z"],["dc.date.issued","2005"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13255"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.title","Insight into the structure and mechanism of the reversible photoswitch of a fluorescent protein: A multi-departmental research approach"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","643a"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","96"],["dc.contributor.author","Puchner, Elias M."],["dc.contributor.author","Alexandrovich, Alexander"],["dc.contributor.author","Kho, Ay L."],["dc.contributor.author","Hensen, Ulf"],["dc.contributor.author","Schäfer, Lars V."],["dc.contributor.author","Brandmeier, Birgit"],["dc.contributor.author","Gräter, Frauke"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Gautel, Mathias"],["dc.contributor.author","Gaub, Hermann E."],["dc.date.accessioned","2022-03-01T11:44:52Z"],["dc.date.available","2022-03-01T11:44:52Z"],["dc.date.issued","2009"],["dc.identifier.doi","10.1016/j.bpj.2008.12.3401"],["dc.identifier.pii","S0006349508036400"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103146"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0006-3495"],["dc.title","Single-Molecule Force Spectroscopy Reveals the Function of Titin Kinase as Force Sensor"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","MPIbpc News"],["dc.bibliographiccitation.lastpage","4"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Andresen, Martin"],["dc.contributor.author","Wahl, Markus C."],["dc.contributor.author","Stiel, André C."],["dc.contributor.author","Gräter, Frauke"],["dc.contributor.author","Schäfer, Lars V."],["dc.contributor.author","Trowitzsch, Simon"],["dc.contributor.author","Weber, Gert"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Hell, Stefan Walter"],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2018-02-09T07:06:40Z"],["dc.date.available","2018-02-09T07:06:40Z"],["dc.date.issued","2005"],["dc.description.abstract","Schaltbare Proteine, die sich durch Be- strahlung mit sichtbarem Licht reversibel zwischen einem fluoreszierenden ‚Ein’- und einem nicht-fl uoreszierenden ‚Aus’- Zustand hin und herschalten lassen, sind erst seit wenigen Jahren bekannt. Derzeit sind mit den Proteinen asFP595 und Dron- pa erst zwei Vertreter solcher reversibel schaltbaren fl uoreszierenden Proteine (RSFPs) beschrieben worden. Nichts- destotrotz verspricht diese neue Protein- klasse aufgrund ihrer einzigartigen Eigen- schaften bereits jetzt eine Vielzahl interes- santer Anwendungsmöglichkeiten. Das Protein asFP595, dessen Schalt- mechanismus wir in dieser Studie unter- sucht haben, kommt normalerweise in den Tentakelspitzen der Wachsrose Anemonia sulcata vor, einer Seeanemone, die in den lichtdurchfluteten Flachwasser- bereichen des Mittelmeers und des Nord- atlantiks lebt. asFP595 wird durch Be- leuchtung mit grünem Licht von einem nicht-fluoreszierenden ‚Aus’-Zustand in einen fluoreszierenden ‚Ein’-Zustand ver- setzt. Von diesem ‚Ein’-Zustand fällt es spontan in den ‚Aus’-Zustand zurück, kann aber auch durch Beleuchtung mit blauem Licht zurückgeschaltet werden. Dieses lichtgetriebene Schalten ist rever- sibel und viele Male wiederholbar. In einer gemeinsamen Studie dreier Abteilungen haben wir die molekulare Struktur von asFP595 bestimmt und wesentliche Teile des Schaltmechanismus aufgeklärt. Diese Untersuchungen haben gezeigt, dass nach der Absorption eines grünen Photons das asFP595-Chromophor von einer Trans- in eine Cis-Position isomerisiert. Molekular- dynamik-Rechnungen deuten an, dass das Chromophor bei dieser lichtinduzierten Reaktion eine ‚Hula-Twist’-Bewegung macht. Bei dieser Bewegung dreht sich in erster Linie die Methin-Brücke, wel- che die beiden aromatischen Ringe des Chromophors verknüpft. Tatsächlich ändert das Chromophor während des Hula-Twists seine Position lediglich um 3 x 10-10 Meter. Diese winzige Änderung reicht aus, um aus dem nicht-fluoreszierenden ein fluo- reszierendes Protein zu machen. Diese neuen Erkenntnisse über die Struktur und den Schaltmechanismus des Prote- ins sollten es zukünftig ermöglichen, mit Hilfe von gerichteten molekularbiologi- schen Ansätzen das Protein für weitere Anwendungen zu optimieren. Denkbare Einsatzbereiche eines solchen modifizier- ten asFP595 reichen von der höchstauf- lösenden Fluoreszenzmikroskopie bis hin zum Einsatz als Datenspeicher."],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/12069"],["dc.language.iso","en"],["dc.language.iso","de"],["dc.notes.status","final"],["dc.title","Insight into the structure and mechanism of the reversible photoswitch of a fl uorescent protein"],["dc.title.subtitle","A multi-departmental research approach"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]