Oxidized arachidonic and adrenic PEs navigate cells to ferroptosis

November 14th, 2016 by Valerian E Kagan

Nature Chemical Biology 13, 81 (2017). doi:10.1038/nchembio.2238

Authors: Valerian E Kagan, Gaowei Mao, Feng Qu, Jose Pedro Friedmann Angeli, Sebastian Doll, Claudette St Croix, Haider Hussain Dar, Bing Liu, Vladimir A Tyurin, Vladimir B Ritov, Alexandr A Kapralov, Andrew A Amoscato, Jianfei Jiang, Tamil Anthonymuthu, Dariush Mohammadyani, Qin Yang, Bettina Proneth, Judith Klein-Seetharaman, Simon Watkins, Ivet Bahar, Joel Greenberger, Rama K Mallampalli, Brent R Stockwell, Yulia Y Tyurina, Marcus Conrad & Hülya Bayır

Elucidation of gibberellin biosynthesis in bacteria reveals convergent evolution

November 14th, 2016 by Ryan S Nett

Nature Chemical Biology 13, 69 (2017). doi:10.1038/nchembio.2232

Authors: Ryan S Nett, Mariana Montanares, Ariana Marcassa, Xuan Lu, Raimund Nagel, Trevor C Charles, Peter Hedden, Maria Cecilia Rojas & Reuben J Peters

  • Posted in Nat Chem Biol, Publications
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A Conserved Tripeptide Sequence at the C-terminus of the Poxvirus DNA Processivity Factor D4 is Essential for Protein Integrity and Function [Microbiology]

November 11th, 2016 by Nuth, M., Guan, H., Ricciardi, R. P.

Vaccinia virus (VACV) is a poxvirus member, and the VACV D4 protein serves both as a uracil-DNA glycosylase (UDG) and as an essential component required for processive DNA synthesis. The VACV A20 protein has no known catalytic function itself, but associates with D4 to form the D4-A20 heterodimer that functions as the poxvirus DNA processivity factor. The heterodimer enables the DNA polymerase to efficiently synthesize extended strands of DNA. Upon characterizing the interaction between D4 and A20, we observed that the C-terminus of D4 is susceptible to perturbation. Further analysis demonstrated that a conserved hexapeptide stretch at the extreme C-terminus of D4 is essential for maintaining protein integrity, as assessed by its requirement for the production of soluble recombinant protein that is functional in processive DNA synthesis. From the known crystal structures of D4, the C-terminal hexapeptide is shown to make intramolecular contact with residues spanning the protein's inner core. Our mutational analysis revealed that a tripeptide motif (215-GFI-217) within the hexapeptide comprises apparent residues necessary for the contact. Prediction of protein disorder identified the hexapeptide and several regions upstream of Gly-215 that comprise residues of the interface surfaces of the D4-A20 heterodimer. Our study suggests that 215-GFI-217 anchors these potentially dynamic upstream regions of the protein in order to maintain protein integrity. Unlike UDGs from diverse sources, where the C-termini are disordered and do not form comparable intramolecular contacts, this feature may be unique to orthopoxviruses.
  • Posted in Journal of Biological Chemistry, Publications
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Cyanobacterial Surface Display System Mediates Engineered Interspecies and Abiotic Binding

November 9th, 2016 by Derek T. Fedeson and Daniel C. Ducat

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ACS Synthetic Biology
DOI: 10.1021/acssynbio.6b00254

Reproducibility of High-Throughput Plate-Reader Experiments in Synthetic Biology

November 9th, 2016 by Michael Chavez, Jonathan Ho and Cheemeng Tan

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ACS Synthetic Biology
DOI: 10.1021/acssynbio.6b00198

Temporal Analysis of PP2A Phosphatase Activity During Insulin Stimulation Using a Direct Activity Probe

November 7th, 2016 by Jon R. Beck, Tiffany Truong and Cliff I. Stains

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ACS Chemical Biology
DOI: 10.1021/acschembio.6b00697
  • Posted in ACS Chemical Biology, Publications
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Host Cell Interactions Are a Significant Barrier to the Clinical Utility of Peptide Antibiotics

November 7th, 2016 by Charles G. Starr, Jing He and William C. Wimley

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ACS Chemical Biology
DOI: 10.1021/acschembio.6b00843

Identification of G-quadruplexes in long functional RNAs using 7-deazaguanine RNA

November 7th, 2016 by Carika Weldon

Nature Chemical Biology 13, 18 (2017). doi:10.1038/nchembio.2228

Authors: Carika Weldon, Isabelle Behm-Ansmant, Laurence H Hurley, Glenn A Burley, Christiane Branlant, Ian C Eperon & Cyril Dominguez

RNA G-quadruplex (G4) structures are thought to affect biological processes, including translation and pre-mRNA splicing, but it is not possible at present to demonstrate that they form naturally at specific sequences in long functional RNA molecules. We developed a new strategy, footprinting of long 7-deazaguanine-substituted RNAs (FOLDeR), that allows the formation of G4s to be confirmed in long RNAs and under functional conditions.

  • Posted in Nat Chem Biol, Publications
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DPP8 and DPP9 inhibition induces pro-caspase-1-dependent monocyte and macrophage pyroptosis

November 7th, 2016 by Marian C Okondo

Nature Chemical Biology 13, 46 (2017). doi:10.1038/nchembio.2229

Authors: Marian C Okondo, Darren C Johnson, Ramya Sridharan, Eun Bin Go, Ashley J Chui, Mitchell S Wang, Sarah E Poplawski, Wengen Wu, Yuxin Liu, Jack H Lai, David G Sanford, Michael O Arciprete, Todd R Golub, William W Bachovchin & Daniel A Bachovchin

  • Posted in Nat Chem Biol, Publications
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Inhibition of RAS function through targeting an allosteric regulatory site

November 7th, 2016 by Russell Spencer-Smith

Nature Chemical Biology 13, 62 (2017). doi:10.1038/nchembio.2231

Authors: Russell Spencer-Smith, Akiko Koide, Yong Zhou, Raphael R Eguchi, Fern Sha, Priyanka Gajwani, Dianicha Santana, Ankit Gupta, Miranda Jacobs, Erika Herrero-Garcia, Jacqueline Cobbert, Hugo Lavoie, Matthew Smith, Thanashan Rajakulendran, Evan Dowdell, Mustafa Nazir Okur, Irina Dementieva, Frank Sicheri, Marc Therrien, John F Hancock, Mitsuhiko Ikura, Shohei Koide & John P O'Bryan

  • Posted in Nat Chem Biol, Publications
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