Click-EM for imaging metabolically tagged nonprotein biomolecules

April 25th, 2016 by John T Ngo

Nature Chemical Biology 12, 459 (2016). doi:10.1038/nchembio.2076

Authors: John T Ngo, Stephen R Adams, Thomas J Deerinck, Daniela Boassa, Frances Rodriguez-Rivera, Sakina F Palida, Carolyn R Bertozzi, Mark H Ellisman & Roger Y Tsien

A small molecule mitigates hearing loss in a mouse model of Usher syndrome III

April 25th, 2016 by Kumar N Alagramam

Nature Chemical Biology 12, 444 (2016). doi:10.1038/nchembio.2069

Authors: Kumar N Alagramam, Suhasini R Gopal, Ruishuang Geng, Daniel H-C Chen, Ina Nemet, Richard Lee, Guilian Tian, Masaru Miyagi, Karine F Malagu, Christopher J Lock, William R K Esmieu, Andrew P Owens, Nicola A Lindsay, Krista Ouwehand, Faywell Albertus, David F Fischer, Roland W Bürli, Angus M MacLeod, William E Harte, Krzysztof Palczewski & Yoshikazu Imanishi

  • Posted in Nat Chem Biol, Publications
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A PHGDH inhibitor reveals coordination of serine synthesis and one-carbon unit fate

April 25th, 2016 by Michael E Pacold

Nature Chemical Biology 12, 452 (2016). doi:10.1038/nchembio.2070

Authors: Michael E Pacold, Kyle R Brimacombe, Sze Ham Chan, Jason M Rohde, Caroline A Lewis, Lotteke J Y M Swier, Richard Possemato, Walter W Chen, Lucas B Sullivan, Brian P Fiske, Steve Cho, Elizaveta Freinkman, Kıvanç Birsoy, Monther Abu-Remaileh, Yoav D Shaul, Chieh Min Liu, Minerva Zhou, Min Jung Koh, Haeyoon Chung, Shawn M Davidson, Alba Luengo, Amy Q Wang, Xin Xu, Adam Yasgar, Li Liu, Ganesha Rai, Kenneth D Westover, Matthew G Vander Heiden, Min Shen, Nathanael S Gray, Matthew B Boxer & David M Sabatini

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Inflammation: Dietary stress relief

April 19th, 2016 by Mirella Bucci

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

Author: Mirella Bucci

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

Kinase regulation: Shortening the loop

April 19th, 2016 by Grant Miura

Nature Chemical Biology 12, 305 (2016). doi:10.1038/nchembio.2072

Author: Grant Miura

RNA trafficking: RCas9 lights the way

April 19th, 2016 by Terry L. Sheppard

Nature Chemical Biology 12, 305 (2016). doi:10.1038/nchembio.2074

Author: Terry L. Sheppard

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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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.

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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