The structure of a nucleolytic ribozyme that employs a catalytic metal ion

March 6th, 2017 by Yijin Liu

Nature Chemical Biology 13, 508 (2017). doi:10.1038/nchembio.2333

Authors: Yijin Liu, Timothy J Wilson & David M J Lilley

  • Posted in Nat Chem Biol, Publications
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Total RNA-seq to identify pharmacological effects on specific stages of mRNA synthesis

March 6th, 2017 by Sarah A Boswell

Nature Chemical Biology 13, 501 (2017). doi:10.1038/nchembio.2317

Authors: Sarah A Boswell, Andrew Snavely, Heather M Landry, L Stirling Churchman, Jesse M Gray & Michael Springer

  • Posted in Nat Chem Biol, Publications
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A new genome-mining tool redefines the lasso peptide biosynthetic landscape

February 28th, 2017 by Jonathan I Tietz

Nature Chemical Biology 13, 470 (2017). doi:10.1038/nchembio.2319

Authors: Jonathan I Tietz, Christopher J Schwalen, Parth S Patel, Tucker Maxson, Patricia M Blair, Hua-Chia Tai, Uzma I Zakai & Douglas A Mitchell

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The Arabidopsis O-fucosyltransferase SPINDLY activates nuclear growth repressor DELLA

February 28th, 2017 by Rodolfo Zentella

Nature Chemical Biology 13, 479 (2017). doi:10.1038/nchembio.2320

Authors: Rodolfo Zentella, Ning Sui, Benjamin Barnhill, Wen-Ping Hsieh, Jianhong Hu, Jeffrey Shabanowitz, Michael Boyce, Neil E Olszewski, Pei Zhou, Donald F Hunt & Tai-ping Sun

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Capzimin is a potent and specific inhibitor of proteasome isopeptidase Rpn11

February 28th, 2017 by Jing Li

Nature Chemical Biology 13, 486 (2017). doi:10.1038/nchembio.2326

Authors: Jing Li, Tanya Yakushi, Francesco Parlati, Andrew L Mackinnon, Christian Perez, Yuyong Ma, Kyle P Carter, Sharon Colayco, Gavin Magnuson, Brock Brown, Kevin Nguyen, Stefan Vasile, Eigo Suyama, Layton H Smith, Eduard Sergienko, Anthony B Pinkerton, Thomas D Y Chung, Amy E Palmer, Ian Pass, Sonja Hess, Seth M Cohen & Raymond J Deshaies

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A fully automated flow-based approach for accelerated peptide synthesis

February 28th, 2017 by Alexander J Mijalis

Nature Chemical Biology 13, 464 (2017). doi:10.1038/nchembio.2318

Authors: Alexander J Mijalis, Dale A Thomas, Mark D Simon, Andrea Adamo, Ryan Beaumont, Klavs F Jensen & Bradley L Pentelute

Here we report a fully automated, flow-based approach to solid-phase polypeptide synthesis, with amide bond formation in 7 seconds and total synthesis times of 40 seconds per amino acid residue. Crude peptide purities and isolated yields were comparable to those for standard-batch solid-phase peptide synthesis. At full capacity, this approach can yield tens of thousands of individual 30-mer peptides per year.

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Expanding the product portfolio of fungal type I fatty acid synthases

February 20th, 2017 by Zhiwei Zhu

Nature Chemical Biology 13, 360 (2017). doi:10.1038/nchembio.2301

Authors: Zhiwei Zhu, Yongjin J Zhou, Anastasia Krivoruchko, Martin Grininger, Zongbao K Zhao & Jens Nielsen

Fungal type I fatty acid synthases (FASs) are mega-enzymes with two separated, identical compartments, in which the acyl carrier protein (ACP) domains shuttle substrates to catalytically active sites embedded in the chamber wall. We devised synthetic FASs by integrating heterologous enzymes into the reaction chambers and demonstrated their capability to convert acyl-ACP or acyl-CoA from canonical fatty acid biosynthesis to short/medium-chain fatty acids and methyl ketones.

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Engineering fatty acid synthases for directed polyketide production

February 20th, 2017 by Jan Gajewski

Nature Chemical Biology 13, 363 (2017). doi:10.1038/nchembio.2314

Authors: Jan Gajewski, Floris Buelens, Sascha Serdjukow, Melanie Janßen, Niña Cortina, Helmut Grubmüller & Martin Grininger

In this study, we engineered fatty acid synthases (FAS) for the biosynthesis of short-chain fatty acids and polyketides, guided by a combined in vitro and in silico approach. Along with exploring the synthetic capability of FAS, we aim to build a foundation for efficient protein engineering, with the specific goal of harnessing evolutionarily related megadalton-scale polyketide synthases (PKS) for the tailored production of bioactive natural compounds.

Ligand-promoted protein folding by biased kinetic partitioning

February 20th, 2017 by Karan S Hingorani

Nature Chemical Biology 13, 369 (2017). doi:10.1038/nchembio.2303

Authors: Karan S Hingorani, Matthew C Metcalf, Derrick T Deming, Scott C Garman, Evan T Powers & Lila M Gierasch

Protein folding in cells occurs in the presence of high concentrations of endogenous binding partners, and exogenous binding partners have been exploited as pharmacological chaperones. A combined mathematical modeling and experimental approach shows that a ligand improves the folding of a destabilized protein by biasing the kinetic partitioning between folding and alternative fates (aggregation or degradation). Computationally predicted inhibition of test protein aggregation and degradation as a function of ligand concentration are validated by experiments in two disparate cellular systems.

mRNA localization: If you have to ASH

February 15th, 2017 by Joshua M. Finkelstein

Nature Chemical Biology 13, 243 (2017). doi:10.1038/nchembio.2323

Author: Joshua M. Finkelstein