RNA conformation: Lightening up invisible states

February 16th, 2016 by Yun-Xing Wang

Nature Chemical Biology 12, 126 (2016). doi:10.1038/nchembio.2030

Author: Yun-Xing Wang

The versatility of RNA is achieved in part through its ability to adopt various shapes of structures. A new technology called X-ray scattering interferometry enables the detection of 'invisible' states by lighting up gold pairs tagged to RNA molecules.

Development and application of bond cleavage reactions in bioorthogonal chemistry

February 16th, 2016 by Jie Li

Nature Chemical Biology 12, 129 (2016). doi:10.1038/nchembio.2024

Authors: Jie Li & Peng R Chen

  • Posted in Nat Chem Biol, Publications
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Optogenetics: Follow the PIF

February 16th, 2016 by Grant Miura

Nature Chemical Biology 12, 125 (2016). doi:10.1038/nchembio.2031

Author: Grant Miura

RNA modification: Translating for growth

February 16th, 2016 by Grant Miura

Nature Chemical Biology 12, 125 (2016). doi:10.1038/nchembio.2034

Author: Grant Miura

Target identification: Getting cholesterol out

February 16th, 2016 by Mirella Bucci

Nature Chemical Biology 12, 125 (2016). doi:10.1038/nchembio.2032

Author: Mirella Bucci

Translation: Ribosomes make sweeping arrests

February 16th, 2016 by Diego A Alonzo

Nature Chemical Biology 12, 127 (2016). doi:10.1038/nchembio.2027

Authors: Diego A Alonzo & T Martin Schmeing

The arrest peptides that function with the macrolide antibiotic erythromycin stall translating ribosomes in the presence of the antibiotic, leading to remodeling of the downstream mRNA and enhancement of the translation of resistance genes. Current work suggests that small changes in the nascent peptide dictate the ability of ribosomes to respond to this and other small molecules.

Allostery: A lipid two-step

February 15th, 2016 by Liang Hong

Nature Chemical Biology 12, 202 (2016). doi:10.1038/nchembio.2037

Authors: Liang Hong & Francesco Tombola

A sensor of membrane depolarization controls the activity of a bound enzyme through a novel mechanism involving two sequential voltage-dependent transitions allosterically coupled to changes in the substrate specificity of the catalytic domain.

YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids

February 15th, 2016 by Gaetano Speciale

Nature Chemical Biology 12, 215 (2016). doi:10.1038/nchembio.2023

Authors: Gaetano Speciale, Yi Jin, Gideon J Davies, Spencer J Williams & Ethan D Goddard-Borger

Sulfoquinovose is produced by photosynthetic organisms at a rate of 1010 tons per annum and is degraded by bacteria as a source of carbon and sulfur. We have identified Escherichia coli YihQ as the first dedicated sulfoquinovosidase and the gateway enzyme to sulfoglycolytic pathways. Structural and mutagenesis studies unveiled the sequence signatures for binding the distinguishing sulfonate residue and revealed that sulfoquinovoside degradation is widespread across the tree of life.

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Allosteric substrate switching in a voltage-sensing lipid phosphatase

February 15th, 2016 by Sasha S Grimm

Nature Chemical Biology 12, 261 (2016). doi:10.1038/nchembio.2022

Authors: Sasha S Grimm & Ehud Y Isacoff

  • Posted in Nat Chem Biol, Publications
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Transcriptome-wide mapping reveals reversible and dynamic N1-methyladenosine methylome

February 10th, 2016 by Xiaoyu Li

Nature Chemical Biology 12, 311 (2016). doi:10.1038/nchembio.2040

Authors: Xiaoyu Li, Xushen Xiong, Kun Wang, Lixia Wang, Xiaoting Shu, Shiqing Ma & Chengqi Yi

  • Posted in Nat Chem Biol, Publications
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