Photo‐induced and Rapid Labeling of Tetrazine‐Bearing Proteins via Cyclopropenone‐Caged Bicyclononynes

Mayer, Susanne V.; Murnauer, Anton; Wrisberg, Marie‐Kristin von; Jokisch, Marie‐Lena; Lang, Kathrin

doi:10.1002/ange.201908209

Cited by 19 publications

(11 citation statements)

References 71 publications

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“…For the incorporation of met-ncbK, the pPylT plasmid carrying the tRNA and the Hsp82_D61C gene with an N-terminal GST-and C-terminal His-tag were cotransformed with the pBK plasmid carrying the respective PylRS 88 into E. coli K12. Cells were grown in 2xYT (10 µg/mL tetracycline, 100 µg/mL ampicillin).…”

Section: Methodsmentioning

confidence: 99%

A methylated lysine is a switch point for conformational communication in the chaperone Hsp90

et al. 2020

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Methylation of a conserved lysine in C-terminal domain of the molecular chaperone Hsp90 was shown previously to affect its in vivo function. However, the underlying mechanism remained elusive. Through a combined experimental and computational approach, this study shows that this site is very sensitive to sidechain modifications and crucial for Hsp90 activity in vitro and in vivo. Our results demonstrate that this particular lysine serves as a switch point for the regulation of Hsp90 functions by influencing its conformational cycle, ATPase activity, co-chaperone regulation, and client activation of yeast and human Hsp90. Incorporation of the methylated lysine via genetic code expansion specifically shows that upon modification, the conformational cycle of Hsp90 is altered. Molecular dynamics simulations including the methylated lysine suggest specific conformational changes that are propagated through Hsp90. Thus, methylation of the C-terminal lysine allows a precise allosteric tuning of Hsp90 activity via long distances.

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Section: Methodsmentioning

confidence: 99%

A methylated lysine is a switch point for conformational communication in the chaperone Hsp90

et al. 2020

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“…By genetically introducing a tetrazine group into the outer-membrane OmpC protein, Lang et al used a photo-IEDDAC of a cyclopropenone-caged dibenzoannulated bicyclo-[6.1.0]nonyne probe to realize UV-controllable labelling of tetrazine-bearing OmpC in live E. coli . 57 Carrico et al applied a photo-Staudinger–Bertozzi reaction for spatial labelling of cell-surface azidoglycoproteins in fixed cells and zebrafish. 32 We utilized the visible light-triggered DVPC reaction to label the epidermal growth factor receptor (EGFR) protein on a live cell membrane bound with VE modified Cetuximab ( Fig.…”

Section: Biological Applications Of Photo-controllable Bioorthogonal Reactionsmentioning

confidence: 99%

Photo-controllable bioorthogonal chemistry for spatiotemporal control of bio-targets in living systems

Kong

Zhu

et al. 2020

Chem. Sci.

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The establishment of bioorthogonal chemistry is one of the most significant advances in chemical biology using exogenous chemistry to perturb and study biological processes. Photo-modulation of biological systems has realized temporal and spatial control on biomacromolecules in living systems. The combination of photo-modulation and bioorthogonal chemistry is therefore emerging as a new direction to develop new chemical biological tools with spatiotemporal resolution. This minireview will focus on recent development of bioorthogonal chemistry subject to spatiotemporal control through photo-irradiation. Different strategies to realize photo-control on bioorthogonal bond-forming reactions and biological applications of photo-controllable bioorthogonal reactions will be summarized to give a perspective on how the innovations on photo-chemistry can contribute to the development of optochemical biology. Future trends to develop more optochemical tools based on novel photochemistry will also be discussed to envision the development of chemistry-oriented optochemical biology.

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“…She combines chemical approaches such as light-induced Diels− Alder ligations and cross-linking reactions to control and perturb protein activity and interactions. 23,24 She then shared her lab's recent innovation of inducible, site-specific attachment of ubiquitin to target proteins in living cells, using a combination of unnatural amino acids and sortase-mediated ligation. 25 Dr. Liu spoke about recent developments to reveal the cellular interactome using cross-linking mass spectrometry (XL-MS).…”

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confidence: 99%

Empowering Global Chemical Biology at the Dawn of the New Decade

Hoogendoorn

Aye

2020

ACS Chem. Biol.

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On January 22−24, 2020, scientific luminaries across the far-flung corners of chemical biology gathered in Geneva, Switzerland, to deliver their latest and greatest discoveries in the field. Generously supported by the Swiss National Science Foundation (SNSF), our academic partners, and industrial and journal sponsors, this chemical biology symposium in our opinion will remain memorable for several years to come, not only because of the diversity in scientific topics delivered by our invited eminent speakers as detailed herein, but it is also one-of-a-kind conference which reflected multidimensional balancebalance in age and gender, across these speakers. Such a remarkable speaker line-up doubtless attracted >200 attendees from academia and industry in and around Switzerland and beyond, representing a huge swathe of subfields of science interfacing chemistry and biology. Poster presentations from students and postdocs further spotlighted the exciting diversity in the field: spanning biosynthesis, optochemical genetics, genetic code expansion, lipid chemical biology, redox perturbation, microfluidics screening, membrane signaling, immune modulation, DNA circuits, and synthetic and computational biology. This notable heterogeneity in scientific topics also went hand-in-hand with the diverse representations of student/postdoc trainees from 56 institutions covering 14 countries worldwide, allowing us to witness science as a truly global enterprise.

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Photo‐induced and Rapid Labeling of Tetrazine‐Bearing Proteins via Cyclopropenone‐Caged Bicyclononynes

Cited by 19 publications

References 71 publications

A methylated lysine is a switch point for conformational communication in the chaperone Hsp90

A methylated lysine is a switch point for conformational communication in the chaperone Hsp90

Photo-controllable bioorthogonal chemistry for spatiotemporal control of bio-targets in living systems

Empowering Global Chemical Biology at the Dawn of the New Decade

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