Insights into newly discovered marks and readers of epigenetic information

August 18th, 2016 by Forest H Andrews

Nature Chemical Biology 12, 662 (2016). doi:10.1038/nchembio.2149

Authors: Forest H Andrews, Brian D Strahl & Tatiana G Kutateladze

  • Posted in Nat Chem Biol, Publications
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Innate immunity: A sweet switch

August 18th, 2016 by Terry L. Sheppard

Nature Chemical Biology 12, 657 (2016). doi:10.1038/nchembio.2162

Author: Terry L. Sheppard

Target validation: Switching domains

August 18th, 2016 by Alessio Ciulli

Nature Chemical Biology 12, 659 (2016). doi:10.1038/nchembio.2154

Author: Alessio Ciulli

Chemical probes and drugs often bind to functional domains on disease-relevant proteins. A study suggests a chemical genetic approach to establish on-target effects by swapping the targeted domain, affording resistance to pharmacological inhibition while retaining functionality.

Chemical synthesis: Linking up lysines

August 18th, 2016 by Caitlin Deane

Nature Chemical Biology 12, 657 (2016). doi:10.1038/nchembio.2163

Author: Caitlin Deane

Discovery of allosteric modulators for GABAA receptors by ligand-directed chemistry

August 15th, 2016 by Kei Yamaura

Nature Chemical Biology 12, 822 (2016). doi:10.1038/nchembio.2150

Authors: Kei Yamaura, Shigeki Kiyonaka, Tomohiro Numata, Ryuji Inoue & Itaru Hamachi

  • Posted in Nat Chem Biol, Publications
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TALE proteins search DNA using a rotationally decoupled mechanism

August 15th, 2016 by Luke Cuculis

Nature Chemical Biology 12, 831 (2016). doi:10.1038/nchembio.2152

Authors: Luke Cuculis, Zhanar Abil, Huimin Zhao & Charles M Schroeder

Structural basis of laminin binding to the LARGE glycans on dystroglycan

August 15th, 2016 by David C Briggs

Nature Chemical Biology 12, 810 (2016). doi:10.1038/nchembio.2146

Authors: David C Briggs, Takako Yoshida-Moriguchi, Tianqing Zheng, David Venzke, Mary E Anderson, Andrea Strazzulli, Marco Moracci, Liping Yu, Erhard Hohenester & Kevin P Campbell

  • Posted in Nat Chem Biol, Publications
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Cellularly active N-hydroxyurea FEN1 inhibitors block substrate entry to the active site

August 15th, 2016 by Jack C Exell

Nature Chemical Biology 12, 815 (2016). doi:10.1038/nchembio.2148

Authors: Jack C Exell, Mark J Thompson, L David Finger, Steven J Shaw, Judit Debreczeni, Thomas A Ward, Claire McWhirter, Catrine L B Siöberg, Daniel Martinez Molina, W Mark Abbott, Clifford D Jones, J Willem M Nissink, Stephen T Durant & Jane A Grasby

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A Glutaredoxin-BolA Complex Serves as an Iron-Sulfur Cluster Chaperone for the Cytosolic Cluster Assembly Machinery [Metabolism]

August 12th, 2016 by Frey, A. G., Palenchar, D. J., Wildemann, J. D., Philpott, C. C.

Cells contain hundreds of proteins that require iron cofactors for activity. Iron cofactors are synthesized in the cell, but the pathways involved in distributing heme, iron-sulfur clusters, and ferrous/ferric ions to apo-proteins remain incompletely defined. In particular, cytosolic monothiol glutaredoxins and BolA-like proteins have been identified as [2Fe-2S]-coordinating complexes in vitro and iron-regulatory proteins in fungi, but it is not clear how these proteins function in mammalian systems or how this complex might affect Fe-S proteins or the cytosolic Fe-S assembly machinery. To explore these questions, we use quantitative immunoprecipitation and live-cell, proximity-dependent biotinylation, to monitor interactions between Glrx3, BolA2, and components of the cytosolic iron-sulfur cluster assembly system. We characterize cytosolic Glrx3-BolA2 as a [2Fe-2S] chaperone complex in human cells. Unlike complexes formed by fungal orthologs, human Glrx3-BolA2 interaction required the coordination of Fe-S clusters, while Glrx3 homodimer formation did not. Cellular Glrx3-BolA2 complexes increased 6-8-fold in response to increasing iron, forming a rapidly-expandable pool of Fe-S clusters. Fe-S coordination by Glrx3-BolA2 did not depend on Ciapin1 or Ciao1, proteins that bind Glrx3 and are involved in cytosolic Fe-S cluster assembly and distribution. Instead, Glrx3 and BolA2 bound and facilitated Fe-S incorporation into Ciapin1, a [2Fe-2S] protein functioning early in the cytosolic Fe-S assembly pathway. Thus, Glrx3-BolA is a [2Fe-2S] chaperone complex capable of transferring [2Fe-2S] clusters to apo-proteins in human cells.

DFT Study on Enzyme Turnover Including Proton and Electron Transfers of Copper-Containing Nitrite Reductase

August 9th, 2016 by Masami Lintuluoto and Juha M. Lintuluoto

TOC Graphic

Biochemistry
DOI: 10.1021/acs.biochem.6b00423