A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo

June 19th, 2017 by Dario Mizrachi

Nature Chemical Biology 13, 1022 (2017). doi:10.1038/nchembio.2409

Authors: Dario Mizrachi, Michael-Paul Robinson, Guoping Ren, Na Ke, Mehmet Berkmen & Matthew P DeLisa

  • Posted in Nat Chem Biol, Publications
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Nucleation and growth of a bacterial functional amyloid at single-fiber resolution

June 19th, 2017 by Mike Sleutel

Nature Chemical Biology 13, 902 (2017). doi:10.1038/nchembio.2413

Authors: Mike Sleutel, Imke Van den Broeck, Nani Van Gerven, Cécile Feuillie, Wim Jonckheere, Claire Valotteau, Yves F Dufrêne & Han Remaut

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Cpf1 proteins excise CRISPR RNAs from mRNA transcripts in mammalian cells

June 19th, 2017 by Guocai Zhong

Nature Chemical Biology 13, 839 (2017). doi:10.1038/nchembio.2410

Authors: Guocai Zhong, Haimin Wang, Yujun Li, Mai H Tran & Michael Farzan

Cpf1 is a CRISPR effector protein that has greater specificity than Streptococcus pyogenes Cas9 (SpCas9) in genome-editing applications. Here we show that Lachnospiraceae bacterium (Lb) and Acidaminococus sp. (As) Cpf1 orthologs have RNase activities that can excise multiple CRISPR RNAs (crRNAs) from a single RNA polymerase II–driven RNA transcript expressed in mammalian cells. This property simplifies modification of multiple genomic targets and can be used to increase the efficiency of Cpf1-mediated editing.

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A heme-dependent enzyme forms the nitrogen–nitrogen bond in piperazate

June 19th, 2017 by Yi-Ling Du

Nature Chemical Biology 13, 836 (2017). doi:10.1038/nchembio.2411

Authors: Yi-Ling Du, Hai-Yan He, Melanie A Higgins & Katherine S Ryan

Molecules containing a nitrogen–nitrogen (N–N) linkage have a variety of structures and biological activities; however, no enzyme has yet been demonstrated to catalyze N–N bond formation in an organic molecule. Here we report that the heme-dependent enzyme KtzT from Kutzneria sp. 744 catalyzes N–N bond formation in the biosynthesis of piperazate, a building block for nonribosomal peptides.

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A scaffold protein that chaperones a cysteine-sulfenic acid in H2O2 signaling

June 19th, 2017 by Antoine Bersweiler

Nature Chemical Biology 13, 909 (2017). doi:10.1038/nchembio.2412

Authors: Antoine Bersweiler, Benoît D'Autréaux, Hortense Mazon, Alexandre Kriznik, Gemma Belli, Agnès Delaunay-Moisan, Michel B Toledano & Sophie Rahuel-Clermont

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Genetically encoding phosphotyrosine and its nonhydrolyzable analog in bacteria

June 12th, 2017 by Xiaozhou Luo

Nature Chemical Biology 13, 845 (2017). doi:10.1038/nchembio.2405

Authors: Xiaozhou Luo, Guangsen Fu, Rongsheng E Wang, Xueyong Zhu, Claudio Zambaldo, Renhe Liu, Tao Liu, Xiaoxuan Lyu, Jintang Du, Weimin Xuan, Anzhi Yao, Sean A Reed, Mingchao Kang, Yuhan Zhang, Hui Guo, Chunhui Huang, Peng-Yu Yang, Ian A Wilson, Peter G Schultz & Feng Wang

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A mutant O-GlcNAcase enriches Drosophila developmental regulators

June 12th, 2017 by Nithya Selvan

Nature Chemical Biology 13, 882 (2017). doi:10.1038/nchembio.2404

Authors: Nithya Selvan, Ritchie Williamson, Daniel Mariappa, David G Campbell, Robert Gourlay, Andrew T Ferenbach, Tonia Aristotelous, Iva Hopkins-Navratilova, Matthias Trost & Daan M F van Aalten

A front-face ‘SNi synthase’ engineered from a retaining ‘double-SN2’ hydrolase

June 12th, 2017 by Javier Iglesias-Fernández

Nature Chemical Biology 13, 874 (2017). doi:10.1038/nchembio.2394

Authors: Javier Iglesias-Fernández, Susan M Hancock, Seung Seo Lee, Maola Khan, Jo Kirkpatrick, Neil J Oldham, Katherine McAuley, Anthony Fordham-Skelton, Carme Rovira & Benjamin G Davis

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A scalable platform to identify fungal secondary metabolites and their gene clusters

June 12th, 2017 by Kenneth D Clevenger

Nature Chemical Biology 13, 895 (2017). doi:10.1038/nchembio.2408

Authors: Kenneth D Clevenger, Jin Woo Bok, Rosa Ye, Galen P Miley, Maria H Verdan, Thomas Velk, Cynthia Chen, KaHoua Yang, Matthew T Robey, Peng Gao, Matthew Lamprecht, Paul M Thomas, Md Nurul Islam, Jonathan M Palmer, Chengcang C Wu, Nancy P Keller & Neil L Kelleher

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Site-specific incorporation of phosphotyrosine using an expanded genetic code

June 12th, 2017 by Christian Hoppmann

Nature Chemical Biology 13, 842 (2017). doi:10.1038/nchembio.2406

Authors: Christian Hoppmann, Allison Wong, Bing Yang, Shuwei Li, Tony Hunter, Kevan M Shokat & Lei Wang

Access to phosphoproteins with stoichiometric and site-specific phosphorylation status is key to understanding the role of protein phosphorylation. Here we report an efficient method to generate pure, active phosphotyrosine-containing proteins by genetically encoding a stable phosphotyrosine analog that is convertible to native phosphotyrosine. We demonstrate its general compatibility with proteins of various sizes, phosphotyrosine sites and functions, and reveal a possible role of tyrosine phosphorylation in negative regulation of ubiquitination.

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