Nature Chemical Biology Contents: April 2016, Volume 12 No 4 pp 201 - 304

If you are unable to see the message below, click here to view.

TABLE OF CONTENTS April 2016 Volume 12, Issue 4 Research Highlights News and Views Review Brief Communication Articles Errata Corrigenda Subscribe   Facebook   RSS   Recommend to library   Twitter   Advertisement npj Systems Biology and Applications is a new online, open access, multi- and cross- disciplinary journal dedicated to publishing finest research on systems biology and all its approaches. Read the latest featured article:  Not just a colourful metaphor: modelling the landscape of cellular development using Hopfield networks    Advertisement All content now free to access including archives! Nature Communications is an open access journal that publishes high-quality research from all areas of the natural sciences. Papers published by the journal represent important advances of significance to specialists within each subject area including chemistry. Visit the website to explore ALL the content available within your field.    Research Highlights Top Host-microbe interactions: Intake control | Transcription: 7SK's enhanced roles | Signal transduction: Lowered exchange rates | Drug discovery: One without the other News and Views Top Allostery: A lipid two-step   pp202 - 203 Liang Hong and Francesco Tombola doi:10.1038/nchembio.2037 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. See also: Article by Grimm & Isacoff Host-pathogen interactions: A cholera surveillance system   pp203 - 204 Aaron T Wright doi:10.1038/nchembio.2039 Bacterial pathogen-secreted proteases may have a key role in inhibiting a potentially widespread host-pathogen interaction. Activity-based protein profiling enabled the identification of a major Vibrio cholerae serine protease that limits the ability of a host-derived intestinal lectin to bind to the bacterial pathogen in vivo. See also: Article by Hatzios et al. Cell division: TIPs for shaping Aurora B activity   pp204 - 205 George Zachos doi:10.1038/nchembio.2041 Cdk1 links mitotic entry to faithful chromosome segregation by activating the acetyltransferase TIP60. Acetylation of Aurora B kinase by TIP60 protects Aurora B's activation loop from dephosphorylation by the PP2A phosphatase to ensure robust Aurora B activation. See also: Article by Mo et al. Motor proteins: Kinesin's gait captured   pp206 - 207 Erwin J G Peterman doi:10.1038/nchembio.2038 Kinesin is a motor protein that drives intracellular transport by stepping along microtubules in a hand-over-hand manner. Advanced dark-field microscopy has made it possible to capture the gait of this motor with unprecedented resolution. See also: Article by Isojima et al. Chemical Biology JOBS of the week Institute Assoc Scientist I In Vitro Pharm The University of Texas MD Anderson Cancer Center Research Scientist I, Calcium Biology Broad Institute Two associate senior lecturers in peptide pharmaceuticals Uppsala University Postdoctoral Research Associate University of Illinois Chicago College of Medicine Postdoc in biochemistry, chemistry or biology University Hospital of Muenster More Science jobs from Chemical Biology EVENT EMBO Conference: Chemical Biology 2016 31 August - 3 September 2016 Heidelberg, Germany More science events from Review Top Toxin-antitoxin systems in bacterial growth arrest and persistence   pp208 - 214 Rebecca Page and Wolfgang Peti doi:10.1038/nchembio.2044 This Review article highlights bacterial toxin-antitoxin system components, their function and the mechanisms they use to affect diverse physiological functions and conditions, including dormancy and entry and exit from the persistent state defined by a high tolerance to antibiotics. Brief Communication Top YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids   pp215 - 217 Gaetano Speciale, Yi Jin, Gideon J Davies, Spencer J Williams and Ethan D Goddard-Borger doi:10.1038/nchembio.2023 YihQ hydrolyzes the glycosidic linkage in sulfoquinovosyl diacylglyceride (SQDG) to form sulfoquinovose (SQ). Crystal structure analysis reveals active site residues required for the specificity of YihQ for SQ and allows the identification of other YihQ homologs. Chemical compounds Articles Top Discovery of tumor-specific irreversible inhibitors of stearoyl CoA desaturase   pp218 - 225 Panayotis C Theodoropoulos, Stephen S Gonzales, Sarah E Winterton, Carlos Rodriguez-Navas, John S McKnight et al. doi:10.1038/nchembio.2016 Two chemical series, oxalamides and benozothiazoles, produced toxicity in particular lung cancer cells. These compounds were metabolized in these sensitive cells by the cytochrome P450 enzyme CYP4F11 into potent inhibitors of stearoyl CoA desaturase. Chemical compounds Acetylation of Aurora B by TIP60 ensures accurate chromosomal segregation   pp226 - 232 Fei Mo, Xiaoxuan Zhuang, Xing Liu, Phil Y Yao, Bo Qin et al. doi:10.1038/nchembio.2017 The cell cycle regulator CDK1 phosphorylates the acetyltransferase TIP60, which subsequently acetylates the mitotic regulator Aurora B to ensure chromosomal segregation. Aurora B acetylation prevents inactivation by PP2A-mediated dephosphorylation. See also: News and Views by Zachos Assembly and clustering of natural antibiotics guides target identification   pp233 - 239 Chad W Johnston, Michael A Skinnider, Chris A Dejong, Philip N Rees, Gregory M Chen et al. doi:10.1038/nchembio.2018 A retrobiosynthetic algorithm that relates known antibiotics by the similarities of their biosynthetic pathways to cluster them into distinct classes. Focusing on the telomycins helps to define the mechanism of action of this antibiotic class. Chemical compounds A proactive role of water molecules in acceptor recognition by protein O-fucosyltransferase 2   pp240 - 246 Jessika Valero-Gonzalez, Christina Leonhard-Melief, Erandi Lira-Navarrete, Gonzalo Jimenez-Oses, Cristina Hernandez-Ruiz et al. doi:10.1038/nchembio.2019 A structural and functional study including a mutational analysis of C. elegans POFUT2 with GDP and a peptide substrate helps explain how this and other fucosyltransferases recognize protein substrates with diverse sequences. Engineering nonphosphorylative metabolism to generate lignocellulose-derived products   pp247 - 253 Yi-Shu Tai, Mingyong Xiong, Pooja Jambunathan, Jingyu Wang, Jilong Wang et al. doi:10.1038/nchembio.2020 Plant biomass provides carbon sources for production of high-value chemical products. Metabolic engineering of a pathway in Escherichia coli that converts pentoses and galacturonate to tricarboxylic acid cycle intermediates provides an efficient route to 1,4-butanediol. A transcription activator-like effector (TALE) induction system mediated by proteolysis   pp254 - 260 Matthew F Copeland, Mark C Politz, Charles B Johnson, Andrew L Markley and Brian F Pfleger doi:10.1038/nchembio.2021 An inducible transcription activator-like effector (TALE) system was developed by inserting tobacco-etch virus (TEV) protease recognition sites into the TALE backbone. The expression of TEV protease degrades the TALE, derepressing plasmid and chromosomal gene expression in Escherichia coli. Allosteric substrate switching in a voltage-sensing lipid phosphatase   pp261 - 267 Sasha S Grimm and Ehud Y Isacoff doi:10.1038/nchembio.2022 The activity of the voltage-sensitive phosphatase from Ciona intestinalis, VSP, towards PIP3 and PIP2 is dictated by the sequential switching between two active conformations of the phosphatase domain that is also correlated with conformational changes in the voltage sensor. See also: News and Views by Hong & Tombola Chemoproteomic profiling of host and pathogen enzymes active in cholera   pp268 - 274 Stavroula K Hatzios, Soren Abel, Julianne Martell, Troy Hubbard, Jumpei Sasabe et al. doi:10.1038/nchembio.2025 Four secreted bacterial serine hydrolases found by an ABPP approach in Vibrio cholerae-infected rabbits, and one in human infection, regulate the levels of intelectin, an intestinal lectin that binds V. cholerae during infection and may facilitate bacterial surveillance in the intestine. See also: News and Views by Wright Pooled screening for antiproliferative inhibitors of protein-protein interactions   pp275 - 281 Satra Nim, Jouhyun Jeon, Carles Corbi-Verge, Moon-Hyeong Seo, Ylva Ivarsson et al. doi:10.1038/nchembio.2026 A high-throughput strategy utilizes a pooled lentiviral approach consisting of a library of 50,000 peptide binding motifs to identify peptide inhibitors of protein-protein interactions that decrease viability in a pancreatic cancer cell line. Autopalmitoylation of TEAD proteins regulates transcriptional output of the Hippo pathway   pp282 - 289 PuiYee Chan, Xiao Han, Baohui Zheng, Michael DeRan, Jianzhong Yu et al. doi:10.1038/nchembio.2036 Biochemical assays using activity-based chemical probes revealed that the Hippo pathway transcription factor TEAD undergoes autopalmitoylation to ensure binding to YAP/TAZ and promote muscle differentiation and tissue growth. Direct observation of intermediate states during the stepping motion of kinesin-1   pp290 - 297 Hiroshi Isojima, Ryota Iino, Yamato Niitani, Hiroyuki Noji and Michio Tomishige doi:10.1038/nchembio.2028 Laser-based dark field microscopy imaging of a gold-labeled kinesin head during microtubule movement reveals a rightward displacement of unbound kinesin mediated by increased tension in the neck linker. See also: News and Views by Peterman The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases   pp298 - 303 Kristian E H Frandsen, Thomas J Simmons, Paul Dupree, Jens-Christian N Poulsen, Glyn R Hemsworth et al. doi:10.1038/nchembio.2029 Lytic polysaccharide monooxygenases (LPMOs) are a class of copper-dependent enzymes that oxidatively degrade polysaccharides and find use in industrial processing of lignocellulose. Crystallographic and spectroscopic studies define how LPMOs recognize their oligosaccharide substrates and mediate oxidative cleavage. Chemical compounds Corrigenda Top Corrigendum: Frequency and amplitude control of cortical oscillations by phosphoinositide waves   p304 Ding Xiong, Shengping Xiao, Su Guo, Qingsong Lin, Fubito Nakatsu et al. doi:10.1038/nchembio0416-304b Corrigendum: SMN2 splice modulators enhance U1-pre-mRNA association and rescue SMA mice   p304 James Palacino, Susanne E Swalley, Cheng Song, Atwood K Cheung, Lei Shu et al. doi:10.1038/nchembio0416-304c Errata Top Erratum: February 2016 cover caption   p304 doi:10.1038/nchembio0416-304a Erratum: ANTIBACTERIALS: Stressing out dormancy   p304 Grant Miura doi:10.1038/nchembio0416-304d Top Natureevents is a fully searchable, multi-disciplinary database designed to maximise exposure for events organisers. The contents of the Natureevents Directory are now live. The digital version is available here. Find the latest scientific conferences, courses, meetings and symposia on natureevents.com. For event advertising opportunities across the Nature Publishing Group portfolio please contact natureevents@nature.com More Nature Events

You have been sent this Table of Contents Alert because you have opted in to receive it. You can change or discontinue your e-mail alerts at any time, by modifying your preferences on your nature.com account at: www.nature.com/myaccount (You will need to log in to be recognised as a nature.com registrant) For further technical assistance, please contact our registration department For print subscription enquiries, please contact our subscription department For other enquiries, please contact our customer feedback department Nature Publishing Group | One New York Plaza, Suite 4500 | New York | NY 10004-1562 | USA Nature Publishing Group's worldwide offices: London - Paris - Munich - New Delhi - Tokyo - Melbourne San Diego - San Francisco - Washington - New York - Boston Macmillan Publishers Limited is a company incorporated in England and Wales under company number 785998 and whose registered office is located at Brunel Road, Houndmills, Basingstoke, Hampshire RG21 6XS. © 2016 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.