Nature Chemical Biology Contents: January 2015, Volume 11 No 1 pp 1 - 89

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

TABLE OF CONTENTS January 2015 Volume 11, Issue 1 Editorial Research Highlights News and Views Perspective Brief Communication Articles Subscribe   Facebook   RSS   Recommend to library   Twitter   Advertisement Nature Communications is now fully open access All new submissions to Nature Communications, if accepted, will be published open access and an article processing charge will apply. For more information visit the website. Many research funders and institutions make funds available to pay open access APCs: please consult our open access funding page to check if your funder or institution has funding available. For advice on whether you are eligible for APC funding and help in approaching funders and institutions please contact us at openaccess@nature.com   Editorial Top Food for thought   p1 doi:10.1038/nchembio.1730 Chemical biology has much to contribute to the global effort to reduce hunger, improve food safety and support sustainable agriculture. Research Highlights Top Biomaterials: Lectins lay the groundwork | Host-viral interactions: Hosting encounters | Glycosylation: A new regulator | Ischemia: Succinate comes up ROSes | Nitrogen metabolism: Plants pocket glutamine | Metals: Regulate good times, c'mon! News and Views Top Enzyme regulation: A thiol switch opens the gate   pp4 - 5 Haike Antelmann doi:10.1038/nchembio.1698 AAA+ proteases are quality control machineries consisting of substrate-binding ATPase modules for protein unfolding and a proteolytic chamber. New research now shows a redox switch in the Escherichia coli Lon protease that controls this process, widening the exit pore and activating proteolysis during transition from anaerobic to aerobic environments. See also: Article by Nishii et al. Redox biology: Signaling via a peroxiredoxin sensor   pp5 - 6 Christine C Winterbourn and Mark B Hampton doi:10.1038/nchembio.1722 Hydrogen peroxide regulates cell signaling pathways through oxidation of specific thiol proteins. A new study describes a relay system involving peroxiredoxin 2 as a peroxide sensor that oxidizes the mammalian transcription factor STAT3 via a mixed disulfide intermediate. See also: Article by Sobotta et al. Protein disorder: Wagging a tail at ubiquitin   pp7 - 8 Tanja Mittag and Melissa R Marzahn doi:10.1038/nchembio.1716 The ubiquitin-conjugating enzyme Ube2w monoubiquitinates proteins with disordered N termini and may target lysine-less proteins for degradation. See also: Article by Vittal et al. Chemical Biology JOBS of the week Tenure-Track Assistant Professorship in Chemistry and Chemical Biology Harvard University Postdoctoral Associate Chemistry and Chemical Biology Yale University Faculty Position - Tenure Track Whitehead Institute and MIT Funded PhD Studentships London Interdisciplinary Biosciences PhD Programme More Science jobs from Chemical Biology EVENT Advances & Progress in Drug Design 16 February 2015 London, UK More science events from Perspective Top Targeting mitochondria metabolism for cancer therapy   pp9 - 15 Samuel E Weinberg and Navdeep S Chandel doi:10.1038/nchembio.1712 Understanding how tumor cells utilize metabolic pathways for proliferation may provide useful strategies for combating cancer. A Perspective discusses recent advances in cancer drug development that target specific aspects of mitochondrial biosynthesis and bioenergetics processes. Brief Communication Top Secondary structure reshuffling modulates glycosyltransferase function at the membrane   pp16 - 18 David Giganti, David Albesa-Jové, Saioa Urresti, Ane Rodrigo-Unzueta, Mariano A Martínez et al. doi:10.1038/nchembio.1694 PimA provides an unusual example of conformational flexibility: structural, biophysical and disulfide trapping experiments now show a glycosyltransferase involved in tuberculosis virulence undergoes a major rearrangement upon contact with membranes. Articles Top Terazosin activates Pgk1 and Hsp90 to promote stress resistance   pp19 - 25 Xinping Chen, Chunyue Zhao, Xiaolong Li, Tao Wang, Yizhou Li et al. doi:10.1038/nchembio.1657 The α1-adrenergic receptor antagonist terazosin protects flies and mammalian cells from stress and apoptosis through direct activation of the glycolytic enzyme phosphoglycerate kinase 1, which interacts with Hsp90 to promote ATP consumption. Chemical compounds LRAT-specific domain facilitates vitamin A metabolism by domain swapping in HRASLS3   pp26 - 32 Marcin Golczak, Avery E Sears, Philip D Kiser and Krzysztof Palczewski doi:10.1038/nchembio.1687 A crystal structure of a chimera composed of lipid-metabolizing transmembrane enzymes HRASLS3 and LRAT (which catalyzes esterification of vitamin A) identifies a quaternary structural rearrangement that coincides with formation of a three-dimensionally swapped dimer. Selective inhibitors of the FK506-binding protein 51 by induced fit   pp33 - 37 Steffen Gaali, Alexander Kirschner, Serena Cuboni, Jakob Hartmann, Christian Kozany et al. doi:10.1038/nchembio.1699 Inhibitors of FKBP51 with antidepressive activity are selective over the related FKBP52 and bind FKBP51 by an induced-fit mechanism that causes a conformational change. The analogous conformational change in FKBP52 generates a strained conformation. Chemical compounds Lipid-linked cell wall precursors regulate membrane association of bacterial actin MreB   pp38 - 45 Kathrin Schirner, Ye-Jin Eun, Mike Dion, Yun Luo, John D Helmann et al. doi:10.1038/nchembio.1689 Bacterial MreB forms cytoskeletal filaments, rotating around the cell width, helping to shape cells. Imaging experiments indicate that MreB association with the B. subtilis cell membrane requires the peptidoglycan and wall teichoic acid precursor lipid II. A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis   pp46 - 51 Wataru Nishii, Mutsuko Kukimoto-Niino, Takaho Terada, Mikako Shirouzu, Tomonari Muramatsu et al. doi:10.1038/nchembio.1688 Proteolysis must be carefully controlled to degrade desired targets without causing cellular damage. New data show that Lon protease in Enterobacteriaceae is regulated by a redox-dependent disulfide bond that determines the size of its exit pore. See also: News and Views by Antelmann Non-plastidic, tyrosine-insensitive prephenate dehydrogenases from legumes   pp52 - 57 Craig A Schenck, Siyu Chen, Daniel L Siehl and Hiroshi A Maeda doi:10.1038/nchembio.1693 Biochemical, bioinformatic and genetic evidence uncover a tyrosine biosynthesis pathway in plants that—in contrast to known plant pathways—occurs in the cytosol, is insensitive to tyrosine feedback regulation and uses the traditionally bacterial prephenate dehydrogenase. GSK-3 modulates cellular responses to a broad spectrum of kinase inhibitors   pp58 - 63 Curtis A Thorne, Chonlarat Wichaidit, Adam D Coster, Bruce A Posner, Lani F Wu et al. doi:10.1038/nchembio.1690 The loss of GSK-3 activity alters cellular responsiveness to kinase inhibitors such as mTOR and PLK1. A kinome-wide RNAi screen reveals that GSK-3 interacts with a third of known kinases. Peroxiredoxin-2 and STAT3 form a redox relay for H2O2 signaling   pp64 - 70 Mirko C Sobotta, Willy Liou, Sarah Stöcker, Deepti Talwar, Michael Oehler et al. doi:10.1038/nchembio.1695 A redox relay was identified in mammalian cells where the H2O2-reactive protein peroxiredoxin-2 oxidizes the transcription factor STAT3, resulting in the formation of transcriptionally inactive disulfide-linked oligomers. See also: News and Views by Winterbourn & Hampton A peptide ligase and the ribosome cooperate to synthesize the peptide pheganomycin   pp71 - 76 Motoyoshi Noike, Takashi Matsui, Koichi Ooya, Ikuo Sasaki, Shouta Ohtaki et al. doi:10.1038/nchembio.1697 Peptide natural product backbones are typically made ribosomally or by NRPS machinery. Exploration of pheganomycin biosynthesis defines a third hybrid model in which a grasp ligase joins an NRPS product with a ribosomally produced peptide. Chemical compounds Structural basis for sialic acid–mediated self-recognition by complement factor H   pp77 - 82 Bärbel S Blaum, Jonathan P Hannan, Andrew P Herbert, David Kavanagh, DuÅ¡an Uhrín et al. doi:10.1038/nchembio.1696 The structure of complement regulatory protein factor H in complex with a preferred sialylated trisaccharide and the C3b thioester domain supports the idea of a ternary complex that mediates discrimination between self and nonself in a branch of innate immunity. Intrinsic disorder drives N-terminal ubiquitination by Ube2w   pp83 - 89 Vinayak Vittal, Lei Shi, Dawn M Wenzel, K Matthew Scaglione, Emily D Duncan et al. doi:10.1038/nchembio.1700 An NMR structure reveals that the C terminus of the ubiquitin-conjugating enzyme Ube2w is disordered, leading to specific pairings with disordered substrates; loss of this sequence causes decreased substrate binding and ubiquitin transfer activity. See also: News and Views by Mittag & Marzahn 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 | 75 Varick Street, 9th Floor | New York | NY 10013-1917 | 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. © 2014 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.