Frequency and amplitude control of cortical oscillations by phosphoinositide waves

January 11th, 2016 by Ding Xiong

Nature Chemical Biology 12, 159 (2016). doi:10.1038/nchembio.2000

Authors: Ding Xiong, Shengping Xiao, Su Guo, Qingsong Lin, Fubito Nakatsu & Min Wu

  • Posted in Nat Chem Biol, Publications
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Protonation of a glutamate residue modulates the dynamics of the drug transporter EmrE

January 11th, 2016 by Anindita Gayen

Nature Chemical Biology 12, 141 (2016). doi:10.1038/nchembio.1999

Authors: Anindita Gayen, Maureen Leninger & Nathaniel J Traaseth

  • Posted in Nat Chem Biol, Publications
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Nascent peptide assists the ribosome in recognizing chemically distinct small molecules

January 4th, 2016 by Pulkit Gupta

Nature Chemical Biology 12, 153 (2016). doi:10.1038/nchembio.1998

Authors: Pulkit Gupta, Bo Liu, Dorota Klepacki, Vrinda Gupta, Klaus Schulten, Alexander S Mankin & Nora Vázquez-Laslop

  • Posted in Nat Chem Biol, Publications
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The solution structural ensembles of RNA kink-turn motifs and their protein complexes

January 4th, 2016 by Xuesong Shi

Nature Chemical Biology 12, 146 (2016). doi:10.1038/nchembio.1997

Authors: Xuesong Shi, Lin Huang, David M J Lilley, Pehr B Harbury & Daniel Herschlag

  • Posted in Nat Chem Biol, Publications
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Photo-lysine captures proteins that bind lysine post-translational modifications

December 21st, 2015 by Tangpo Yang

Nature Chemical Biology 12, 70 (2016). doi:10.1038/nchembio.1990

Authors: Tangpo Yang, Xiao-Meng Li, Xiucong Bao, Yi Man Eva Fung & Xiang David Li

Post-translational modifications (PTMs) have key roles in regulating protein-protein interactions in living cells. However, it remains a challenge to identify these PTM-mediated interactions. Here we develop a new lysine-based photo-reactive amino acid, termed photo-lysine. We demonstrate that photo-lysine, which is readily incorporated into proteins by native mammalian translation machinery, can be used to capture and identify proteins that recognize lysine PTMs, including 'readers' and 'erasers' of histone modifications.

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A nitrous acid biosynthetic pathway for diazo group formation in bacteria

December 21st, 2015 by Yoshinori Sugai

Nature Chemical Biology 12, 73 (2016). doi:10.1038/nchembio.1991

Authors: Yoshinori Sugai, Yohei Katsuyama & Yasuo Ohnishi

Although some diazo compounds have bioactivities of medicinal interest, little is known about diazo group formation in nature. Here we describe an unprecedented nitrous acid biosynthetic pathway responsible for the formation of a diazo group in the biosynthesis of the ortho-diazoquinone secondary metabolite cremeomycin in Streptomyces cremeus. This finding provides important insights into the biosynthetic pathways not only for diazo compounds but also for other naturally occurring compounds containing nitrogen-nitrogen bonds.

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Probe discovery: Disentangling gene networks

December 17th, 2015 by Finbarr Hayes

Nature Chemical Biology 12, 3 (2016). doi:10.1038/nchembio.1983

Author: Finbarr Hayes

Cell-wall biogenesis in bacteria involves multiple intersecting gene networks. A powerful approach that allies synthetic lethality with small-molecule discovery has now been used to probe these networks and has revealed that the pathway for D-alanylation of teichoic acids in Staphylococcus aureus is a viable target for new antibacterials.

Microscopy techniques: A localization module

December 17th, 2015 by Mirella Bucci

Nature Chemical Biology 12, 1 (2016). doi:10.1038/nchembio.1994

Author: Mirella Bucci

Protein Design: Getting to the bottom of the TIM barrel

December 17th, 2015 by Vikas Nanda

Nature Chemical Biology 12, 2 (2016). doi:10.1038/nchembio.1987

Author: Vikas Nanda

Natural (βα)8-barrel proteins support diverse catalytic functions and are fertile scaffolds for engineering synthetic enzymes. The atomic-resolution structure determination of a computationally guided, de novo–designed symmetric barrel is a long-awaited advance that opens up new opportunities for enzyme design.

Transcriptional kinases: Less is more (or less)

December 17th, 2015 by Thomas G Boyer

Nature Chemical Biology 12, 4 (2016). doi:10.1038/nchembio.1985

Author: Thomas G Boyer

Two new studies describe potent and selective inhibitors of CDK8/CDK19. Application of these high-quality probes to several cancer models provides new mechanistic insight and reveals functional dichotomy with respect to Mediator kinases in signal-dependent gene regulation, with important implications for targeted cancer therapy.