Kinetochore regulation: Let there be light

August 14th, 2017 by Ana C Figueiredo

Nature Chemical Biology 13, 1058 (2017). doi:10.1038/nchembio.2464

Authors: Ana C Figueiredo & Helder Maiato

Kinetochores form the critical interface with spindle microtubules that accounts for chromosome movement and segregation fidelity during mitosis. Spatial and temporal control of motor protein and checkpoint signaling at kinetochores is now possible with a new set of optogenetic tools.

Engineering Aromatic–Aromatic Interactions To Nucleate Folding in Intrinsically Disordered Regions of Proteins

August 11th, 2017 by Swati Balakrishnan and Siddhartha P. Sarma

TOC Graphic

Biochemistry
DOI: 10.1021/acs.biochem.7b00437

Fibronectin Conformation and Assembly: Analysis of Fibronectin Deletion Mutants and Fibronectin Glomerulopathy (GFND) Mutants

August 10th, 2017 by Tomoo Ohashi, Christopher A. Lemmon and Harold P. Erickson

TOC Graphic

Biochemistry
DOI: 10.1021/acs.biochem.7b00589

Mapping Functionally Important Residues in the Na+/Dicarboxylate Cotransporter, NaDC1

August 10th, 2017 by Claire Colas, Avner Schlessinger and Ana M. Pajor

TOC Graphic

Biochemistry
DOI: 10.1021/acs.biochem.7b00503

Efficient reduction of CO2 by the molybdenum-containing formate dehydrogenase from Cupriavidus necator (Ralstonia eutropha). [Molecular Biophysics]

August 7th, 2017 by Xuejun Yu, Dimitri Niks, Ashok Mulchandani, Russ Hille

The ability of the FdsABG formate dehydrogenase from Cupriavidus necator (formerly known as Ralstonia eutropha) to catalyze the reverse of the physiological reaction, the reduction of CO2 to formate utilizing NADH as electron donor, has been investigated. Contrary to previous studies of this enzyme, we demonstrate that it is in fact effective in catalyzing the reverse reaction, with a kcat of 11 ± 0.4 s-1. We also quantify the stoichiometric accumulation of formic acid as the product of the reaction and demonstrate that the observed kinetic parameters for catalysis in the forward and reverse reaction are thermodynamically consistent, complying with the expected Haldane relationships. Finally, we demonstrate the reaction conditions necessary for gauging the ability of a given formate dehydrogenase or other CO2-utilizing enzyme to catalyze the reverse direction so as to avoid false negative results. In conjunction with our earlier studies on the reaction mechanism of this enzyme (Niks et al. (2016) J. Biol. Chem. 291, 1162- 1174), and on the basis of the present work we conclude that all molybdenum- and tungsten-containing formate dehydrogenases and related enzymes likely operate via a simple hydride transfer mechanism and are effective in catalysing the reversible interconversion of CO2 and formate under the appropriate experimental conditions.
  • Posted in Journal of Biological Chemistry, Publications
  • Comments Off on Efficient reduction of CO2 by the molybdenum-containing formate dehydrogenase from Cupriavidus necator (Ralstonia eutropha). [Molecular Biophysics]

Colibactin assembly line enzymes use S-adenosylmethionine to build a cyclopropane ring

August 7th, 2017 by Li Zha

Nature Chemical Biology 13, 1063 (2017). doi:10.1038/nchembio.2448

Authors: Li Zha, Yindi Jiang, Matthew T Henke, Matthew R Wilson, Jennifer X Wang, Neil L Kelleher & Emily P Balskus

Despite containing an α-amino acid, the versatile cofactor S-adenosylmethionine (SAM) is not a known building block for nonribosomal peptide synthetase (NRPS) assembly lines. Here we report an unusual NRPS module from colibactin biosynthesis that uses SAM for amide bond formation and subsequent cyclopropanation. Our findings showcase a new use for SAM and reveal a novel biosynthetic route to a functional group that likely mediates colibactin's genotoxicity.

  • Posted in Nat Chem Biol, Publications
  • Comments Off on Colibactin assembly line enzymes use S-adenosylmethionine to build a cyclopropane ring

Bisphosphoglycerate mutase controls serine pathway flux via 3-phosphoglycerate

August 7th, 2017 by Rob C Oslund

Nature Chemical Biology 13, 1081 (2017). doi:10.1038/nchembio.2453

Authors: Rob C Oslund, Xiaoyang Su, Michael Haugbro, Jung-Min Kee, Mark Esposito, Yael David, Boyuan Wang, Eva Ge, David H Perlman, Yibin Kang, Tom W Muir & Joshua D Rabinowitz

  • Posted in Nat Chem Biol, Publications
  • Comments Off on Bisphosphoglycerate mutase controls serine pathway flux via 3-phosphoglycerate

A genetically encoded tool for manipulation of NADP+/NADPH in living cells

August 7th, 2017 by Valentin Cracan

Nature Chemical Biology 13, 1088 (2017). doi:10.1038/nchembio.2454

Authors: Valentin Cracan, Denis V Titov, Hongying Shen, Zenon Grabarek & Vamsi K Mootha

  • Posted in Nat Chem Biol, Publications
  • Comments Off on A genetically encoded tool for manipulation of NADP+/NADPH in living cells

Modulating the DNA polymerase β reaction equilibrium to dissect the reverse reaction

July 31st, 2017 by David D Shock

Nature Chemical Biology 13, 1074 (2017). doi:10.1038/nchembio.2450

Authors: David D Shock, Bret D Freudenthal, William A Beard & Samuel H Wilson

  • Posted in Nat Chem Biol, Publications
  • Comments Off on Modulating the DNA polymerase β reaction equilibrium to dissect the reverse reaction

Molecular basis for the unusual ring reconstruction in fungal meroterpenoid biogenesis

July 31st, 2017 by Takahiro Mori

Nature Chemical Biology 13, 1066 (2017). doi:10.1038/nchembio.2443

Authors: Takahiro Mori, Taiki Iwabuchi, Shotaro Hoshino, Hang Wang, Yudai Matsuda & Ikuro Abe

  • Posted in Nat Chem Biol, Publications
  • Comments Off on Molecular basis for the unusual ring reconstruction in fungal meroterpenoid biogenesis