Bright ligand-activatable fluorescent protein for high-quality multicolor live-cell super-resolution microscopy
DC Field | Value | Language |
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dc.contributor.author | Kwon, Jiwoong | - |
dc.contributor.author | Park, Jong-Seok | - |
dc.contributor.author | Kang, Minsu | - |
dc.contributor.author | Choi, Soobin | - |
dc.contributor.author | Park, Jumi | - |
dc.contributor.author | Kim, Gyeong Tae | - |
dc.contributor.author | Lee, Changwook | - |
dc.contributor.author | Cha, Sangwon | - |
dc.contributor.author | Rhee, Hyun-Woo | - |
dc.contributor.author | Shim, Sang-Hee | - |
dc.date.accessioned | 2021-08-31T13:43:03Z | - |
dc.date.available | 2021-08-31T13:43:03Z | - |
dc.date.created | 2021-06-18 | - |
dc.date.issued | 2020-01-14 | - |
dc.identifier.issn | 2041-1723 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/58311 | - |
dc.description.abstract | We introduce UnaG as a green-to-dark photoswitching fluorescent protein capable of high-quality super-resolution imaging with photon numbers equivalent to the brightest photoswitchable red protein. UnaG only fluoresces upon binding of a fluorogenic metabolite, bilirubin, enabling UV-free reversible photoswitching with easily controllable kinetics and low background under Epi illumination. The on- and off-switching rates are controlled by the concentration of the ligand and the excitation light intensity, respectively, where the dissolved oxygen also promotes the off-switching. The photo-oxidation reaction mechanism of bilirubin in UnaG suggests that the lack of ligand-protein covalent bond allows the oxidized ligand to detach from the protein, emptying the binding cavity for rebinding to a fresh ligand molecule. We demonstrate super-resolution single-molecule localization imaging of various subcellular structures genetically encoded with UnaG, which enables facile labeling and simultaneous multicolor imaging of live cells. UnaG has the promise of becoming a default protein for high-performance super-resolution imaging. Photoconvertible proteins occupy two color channels thereby limiting multicolour localisation microscopy applications. Here the authors present UnaG, a new green-to-dark photoswitching fluorescent protein for super-resolution imaging, whose activation is based on a noncovalent binding with bilirubin. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.subject | BILIRUBIN | - |
dc.subject | MOLECULES | - |
dc.subject | MECHANISM | - |
dc.subject | CYTOCHROME-P450 | - |
dc.subject | DEGRADATION | - |
dc.subject | PERFORMANCE | - |
dc.subject | REPORTER | - |
dc.subject | PRODUCTS | - |
dc.subject | BINDING | - |
dc.subject | TAG | - |
dc.title | Bright ligand-activatable fluorescent protein for high-quality multicolor live-cell super-resolution microscopy | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Shim, Sang-Hee | - |
dc.identifier.doi | 10.1038/s41467-019-14067-4 | - |
dc.identifier.scopusid | 2-s2.0-85077874510 | - |
dc.identifier.wosid | 000528906000005 | - |
dc.identifier.bibliographicCitation | NATURE COMMUNICATIONS, v.11, no.1 | - |
dc.relation.isPartOf | NATURE COMMUNICATIONS | - |
dc.citation.title | NATURE COMMUNICATIONS | - |
dc.citation.volume | 11 | - |
dc.citation.number | 1 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.subject.keywordPlus | BILIRUBIN | - |
dc.subject.keywordPlus | MOLECULES | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | CYTOCHROME-P450 | - |
dc.subject.keywordPlus | DEGRADATION | - |
dc.subject.keywordPlus | PERFORMANCE | - |
dc.subject.keywordPlus | REPORTER | - |
dc.subject.keywordPlus | PRODUCTS | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | TAG | - |
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