ACS DIVISION OF BIOLOGICAL CHEMISTRY

September 26th, 2019 by Balaka Mondal and Govardhan Reddy*

September 25th, 2019 by Sang Min Lim*

September 23rd, 2019 by Jason Gaglia†‡ and Stephan Kissler*†‡

September 23rd, 2019 by Junyoung O. Park

Nature Chemical Biology, Published online: 23 September 2019; doi:10.1038/s41589-019-0364-9

A 2H and 13C tracing strategy was used for efficient determination of glycolytic thermodynamics, revealing near-equilibrium glycolytic steps enabling rapid flux adaptation and, in Clostridium cellulolyticum, enhanced ATP yield.

September 23rd, 2019 by Amalie F. Rudolf

Nature Chemical Biology, Published online: 23 September 2019; doi:10.1038/s41589-019-0370-y

Cholesterol can function as both a substrate and an inhibitor of the Hedgehog receptor Patched. Structural analysis and molecular dynamics simulations reveal that cholesterol inhibits Patched by inserting into its extracellular domain

September 23rd, 2019 by Monica E. Neugebauer

Nature Chemical Biology, Published online: 23 September 2019; doi:10.1038/s41589-019-0355-x

Structural characterization of the amino-acid-modifying radical halogenase BesD and identification of new members of this protein family provides insight into the enzymatic mechanism and enables biocatalytic production of halogenated amino acids.

September 20th, 2019 by Huiqing Hu, Tai An, Yasuhiro Kurasawa, Qing Zhou, Ziyin Li

The evolutionarily early divergent human parasite Trypanosoma brucei proliferates through binary cell fission in both its tsetse fly vector and mammalian host. The parasite divides uni-directionally along the longitudinal cell axis from the anterior cell tip toward the posterior cell tip through a mechanism distinct from that in the cells of its human host. Initiation of cytokinesis in T. brucei is regulated by two evolutionarily conserved protein kinases, the Polo-like kinase TbPLK and the Aurora B kinase TbAUK1, and a cohort of trypanosome-specific proteins, including three cytokinesis initiation factors CIF1, CIF2, and CIF3. Here, using RNA interference, in situ epitope tagging of proteins, GST pull-down and co-immunoprecipitation assays, and immunofluorescence and scanning EM microscopy analyses, we report the identification and functional characterization of two trypanosome-specific proteins, FPRC and CIF4. We found that the two proteins co-localize to the distal tips of the new and the old flagellum attachment zones, and are required for cytokinesis initiation. Knockdown of FPRC or CIF4 each disrupted the localization of CIF1, suggesting that they function upstream of CIF1. Moreover, depletion of CIF4 abolished FPRC localization, indicating that CIF4 acts upstream of FPRC. Together, these results identify two new cytokinesis regulators in T. brucei and integrate them into the CIF1-mediated cytokinesis regulatory pathway. These findings highlight the existence of a cytokinesis pathway in T. brucei that is different from that of its mammalian host and therefore suggest that cytokinesis in T. brucei could potentially be exploited as a new drug target.

September 20th, 2019 by Grant Miura

Nature Chemical Biology, Published online: 20 September 2019; doi:10.1038/s41589-019-0376-5

The root of the cause

September 20th, 2019 by Mirella Bucci

Nature Chemical Biology, Published online: 20 September 2019; doi:10.1038/s41589-019-0374-7

A NAMe-tag for ALS

September 20th, 2019 by Yiyun Song

Nature Chemical Biology, Published online: 20 September 2019; doi:10.1038/s41589-019-0375-6

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