Ribozymes: How RNA catalyzes cyclization

September 28th, 2015 by Zhensheng Zhong

Nature Chemical Biology 11, 830 (2015). doi:10.1038/nchembio.1928

Authors: Zhensheng Zhong & Gang Chen

The long-awaited crystal structure of the Varkud satellite (VS) ribozyme dimer provides atomic-level insights into how the VS ribozyme folds and catalyzes RNA circularization during rolling circle replication, as well as revealing convergent evolution used by RNAs to catalyze an SN2 reaction.

Notch-modifying xylosyltransferase structures support an SNi-like retaining mechanism

September 28th, 2015 by Hongjun Yu

Nature Chemical Biology 11, 847 (2015). doi:10.1038/nchembio.1927

Authors: Hongjun Yu, Megumi Takeuchi, Jamie LeBarron, Joshua Kantharia, Erwin London, Hans Bakker, Robert S Haltiwanger, Huilin Li & Hideyuki Takeuchi

  • Posted in Nat Chem Biol, Publications
  • Comments Off on Notch-modifying xylosyltransferase structures support an SNi-like retaining mechanism

Two cytochromes P450 catalyze S-heterocyclizations in cabbage phytoalexin biosynthesis

September 21st, 2015 by Andrew P Klein

Nature Chemical Biology 11, 837 (2015). doi:10.1038/nchembio.1914

Authors: Andrew P Klein & Elizabeth S Sattely

Phytoalexins are abundant in edible crucifers and have important biological activities, yet no dedicated gene for their biosynthesis is known. Here, we report two new cytochromes P450 from Brassica rapa (Chinese cabbage) that catalyze unprecedented S-heterocyclizations in cyclobrassinin and spirobrassinin biosynthesis. Our results provide genetic and biochemical insights into the biosynthesis of a prominent pair of dietary metabolites and have implications for pathway discovery across >20 recently sequenced crucifers.

  • Posted in Nat Chem Biol, Publications
  • Comments Off on Two cytochromes P450 catalyze S-heterocyclizations in cabbage phytoalexin biosynthesis

Translocation-coupled DNA cleavage by the Type ISP restriction-modification enzymes

September 21st, 2015 by Mahesh K Chand

Nature Chemical Biology 11, 870 (2015). doi:10.1038/nchembio.1926

Authors: Mahesh K Chand, Neha Nirwan, Fiona M Diffin, Kara van Aelst, Manasi Kulkarni, Christian Pernstich, Mark D Szczelkun & Kayarat Saikrishnan

  • Posted in Nat Chem Biol, Publications
  • Comments Off on Translocation-coupled DNA cleavage by the Type ISP restriction-modification enzymes

Antibiotic resistance: A minimal measurement

September 17th, 2015 by Mirella Bucci

Nature Chemical Biology 11, 755 (2015). doi:10.1038/nchembio.1923

Author: Mirella Bucci

Searching for harmony in transition-metal signaling

September 17th, 2015 by Christopher J Chang

Nature Chemical Biology 11, 744 (2015). doi:10.1038/nchembio.1913

Author: Christopher J Chang

The recent emergence of signaling roles for transition metals presages a broader contribution of these elements beyond their traditional functions as metabolic cofactors. New chemical approaches to identify the sources, targets and physiologies of transition-metal signaling can help expand understanding of the periodic table in a biological context.

Metabolism: Jump-starting CoA biosynthesis

September 17th, 2015 by Marianne de Villiers

Nature Chemical Biology 11, 757 (2015). doi:10.1038/nchembio.1912

Authors: Marianne de Villiers & Erick Strauss

The essential metabolic cofactor coenzyme A was believed to be produced by biosynthesis from pantothenate in all eukaryotic cells. Rescue experiments in systems depleted of CoA have shown that a phosphorylated CoA biosynthetic intermediate can pass through eukaryotic membranes to serve as an alternative source.

Small-molecule inhibitors: bULKing up mTOR inhibition

September 17th, 2015 by Jonathan M Goodwin

Nature Chemical Biology 11, 758 (2015). doi:10.1038/nchembio.1909

Authors: Jonathan M Goodwin & Leon O Murphy

A new small-molecule inhibitor of the autophagy-initiating kinase ULK1 serves to block a critical survival mechanism activated upon inhibition of mTORC1, potentially enhancing treatment efficacy for mTOR inhibitors currently in clinical trials for cancer treatment.

Host-directed drug therapy for tuberculosis

September 17th, 2015 by Reto Guler

Nature Chemical Biology 11, 748 (2015). doi:10.1038/nchembio.1917

Authors: Reto Guler & Frank Brombacher

Chemical compounds designed to enhance understanding of host-pathogen interaction together with next-generation 'smart drugs' will rationally drive the discovery of promising new host-directed targets against pathogens including Mycobacterium tuberculosis, the causative agent of tuberculosis.

Corrigendum: Structural basis of enzymatic benzene ring reduction

September 17th, 2015 by Tobias Weinert

Nature Chemical Biology 11, 815 (2015). doi:10.1038/nchembio1015-815a

Author: Tobias Weinert, Simona G Huwiler, Johannes W Kung, Sina Weidenweber, Petra Hellwig, Hans-Joachim Stärk, Till Biskup, Stefan Weber, Julien J H Cotelesage, Graham N George, Ulrich Ermler & Matthias Boll