Protein synthesis: Taming transmembrane proteins

April 19th, 2016 by Caitlin Deane

Nature Chemical Biology 12, 305 (2016). doi:10.1038/nchembio.2073

Author: Caitlin Deane

Inflammation: Dietary stress relief

April 19th, 2016 by Mirella Bucci

Nature Chemical Biology 12, 305 (2016). doi:10.1038/nchembio.2075

Author: Mirella Bucci

Light-induced nuclear export reveals rapid dynamics of epigenetic modifications

April 18th, 2016 by Hayretin Yumerefendi

Nature Chemical Biology 12, 399 (2016). doi:10.1038/nchembio.2068

Authors: Hayretin Yumerefendi, Andrew Michael Lerner, Seth Parker Zimmerman, Klaus Hahn, James E Bear, Brian D Strahl & Brian Kuhlman

We engineered a photoactivatable system for rapidly and reversibly exporting proteins from the nucleus by embedding a nuclear export signal in the LOV2 domain from phototropin 1. Fusing the chromatin modifier Bre1 to the photoswitch, we achieved light-dependent control of histone H2B monoubiquitylation in yeast, revealing fast turnover of the ubiquitin mark. Moreover, this inducible system allowed us to dynamically monitor the status of epigenetic modifications dependent on H2B ubiquitylation.

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The Taf14 YEATS domain is a reader of histone crotonylation

April 18th, 2016 by Forest H Andrews

Nature Chemical Biology 12, 396 (2016). doi:10.1038/nchembio.2065

Authors: Forest H Andrews, Stephen A Shinsky, Erin K Shanle, Joseph B Bridgers, Anneliese Gest, Ian K Tsun, Krzysztof Krajewski, Xiaobing Shi, Brian D Strahl & Tatiana G Kutateladze

The discovery of new histone modifications is unfolding at startling rates; however, the identification of effectors capable of interpreting these modifications has lagged behind. Here we report the YEATS domain as an effective reader of histone lysine crotonylation, an epigenetic signature associated with active transcription. We show that the Taf14 YEATS domain engages crotonyllysine via a unique π–π–π-stacking mechanism and that other YEATS domains have crotonyllysine-binding activity.

Real-time monitoring of basal H2O2 levels with peroxiredoxin-based probes

April 18th, 2016 by Bruce Morgan

Nature Chemical Biology 12, 437 (2016). doi:10.1038/nchembio.2067

Authors: Bruce Morgan, Koen Van Laer, Theresa N E Owusu, Daria Ezeriņa, Daniel Pastor-Flores, Prince Saforo Amponsah, Anja Tursch & Tobias P Dick

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Optimized second-generation CRY2–CIB dimerizers and photoactivatable Cre recombinase

April 11th, 2016 by Amir Taslimi

Nature Chemical Biology 12, 425 (2016). doi:10.1038/nchembio.2063

Authors: Amir Taslimi, Brian Zoltowski, Jose G Miranda, Gopal P Pathak, Robert M Hughes & Chandra L Tucker

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Optogenetic oligomerization of Rab GTPases regulates intracellular membrane trafficking

April 11th, 2016 by Mai Khanh Nguyen

Nature Chemical Biology 12, 431 (2016). doi:10.1038/nchembio.2064

Authors: Mai Khanh Nguyen, Cha Yeon Kim, Jin Man Kim, Byung Ouk Park, Sangkyu Lee, Hyerim Park & Won Do Heo

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Plant-like biosynthesis of isoquinoline alkaloids in Aspergillus fumigatus

April 11th, 2016 by Joshua A Baccile

Nature Chemical Biology 12, 419 (2016). doi:10.1038/nchembio.2061

Authors: Joshua A Baccile, Joseph E Spraker, Henry H Le, Eileen Brandenburger, Christian Gomez, Jin Woo Bok, Juliane Macheleidt, Axel A Brakhage, Dirk Hoffmeister, Nancy P Keller & Frank C Schroeder

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A synthetic biochemistry module for production of bio-based chemicals from glucose

April 11th, 2016 by Paul H Opgenorth

Nature Chemical Biology 12, 393 (2016). doi:10.1038/nchembio.2062

Authors: Paul H Opgenorth, Tyler P Korman & James U Bowie

Synthetic biochemistry, the cell-free production of biologically based chemicals, is a potentially high-yield, flexible alternative to in vivo metabolic engineering. To limit costs, cell-free systems must be designed to operate continuously with minimal addition of feedstock chemicals. We describe a robust, efficient synthetic glucose breakdown pathway and implement it for the production of bioplastic. The system's performance suggests that synthetic biochemistry has the potential to become a viable industrial alternative.

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Raft-based interactions of gangliosides with a GPI-anchored receptor

April 4th, 2016 by Naoko Komura

Nature Chemical Biology 12, 402 (2016). doi:10.1038/nchembio.2059

Authors: Naoko Komura, Kenichi G N Suzuki, Hiromune Ando, Miku Konishi, Machi Koikeda, Akihiro Imamura, Rahul Chadda, Takahiro K Fujiwara, Hisae Tsuboi, Ren Sheng, Wonhwa Cho, Koichi Furukawa, Keiko Furukawa, Yoshio Yamauchi, Hideharu Ishida, Akihiro Kusumi & Makoto Kiso