Neurobiology: Tracking the scent

January 19th, 2016 by Catherine Goodman

Nature Chemical Biology 12, 53 (2016). doi:10.1038/nchembio.2011

Author: Catherine Goodman

A topological and conformational stability alphabet for multipass membrane proteins

January 18th, 2016 by Xiang Feng

Nature Chemical Biology 12, 167 (2016). doi:10.1038/nchembio.2001

Authors: Xiang Feng & Patrick Barth

  • Posted in Nat Chem Biol, Publications
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Small-molecule targeting of a diapophytoene desaturase inhibits S. aureus virulence

January 18th, 2016 by Feifei Chen

Nature Chemical Biology 12, 174 (2016). doi:10.1038/nchembio.2003

Authors: Feifei Chen, Hongxia Di, Youxin Wang, Qiao Cao, Bin Xu, Xue Zhang, Nana Yang, Guijie Liu, Cai-Guang Yang, Yong Xu, Hualiang Jiang, Fulin Lian, Naixia Zhang, Jian Li & Lefu Lan

  • Posted in Nat Chem Biol, Publications
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Addicting diverse bacteria to a noncanonical amino acid

January 18th, 2016 by Drew S Tack

Nature Chemical Biology 12, 138 (2016). doi:10.1038/nchembio.2002

Authors: Drew S Tack, Jared W Ellefson, Ross Thyer, Bo Wang, Jimmy Gollihar, Matthew T Forster & Andrew D Ellington

Engineered orthogonal translation systems have greatly enabled the expansion of the genetic code using noncanonical amino acids (NCAAs). However, the impact of NCAAs on organismal evolution remains unclear, in part because it is difficult to force the adoption of new genetic codes in organisms. By reengineering TEM-1 β-lactamase to be dependent on a NCAA, we maintained bacterial NCAA dependence for hundreds of generations without escape.

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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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.

  • 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.

  • Posted in Nat Chem Biol, Publications
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