Metalloproteins: Simple structure, complex function

September 17th, 2015 by Angela Lombardi

Nature Chemical Biology 11, 760 (2015). doi:10.1038/nchembio.1918

Author: Angela Lombardi

The four-helix bundle is a simple structural motif, widespread in nature, that is involved in numerous and fundamental processes. This portfolio is now expanded by the report of a four-helix bundle protein able to store copper for particulate methane monooxygenase, an enzyme that catalyzes methane oxidation.

Plant development: Wave-up call

September 17th, 2015 by Grant Miura

Nature Chemical Biology 11, 754 (2015). doi:10.1038/nchembio.1920

Author: Grant Miura

Riboswitches: Sound the alarm

September 17th, 2015 by Catherine Goodman

Nature Chemical Biology 11, 755 (2015). doi:10.1038/nchembio.1924

Author: Catherine Goodman

Nucleotide metabolism: Salvaging chemotherapy

September 17th, 2015 by Terry L. Sheppard

Nature Chemical Biology 11, 754 (2015). doi:10.1038/nchembio.1921

Author: Terry L. Sheppard

Metals: Calprotectin and iron match up

September 17th, 2015 by Guenter Weiss

Nature Chemical Biology 11, 756 (2015). doi:10.1038/nchembio.1915

Author: Guenter Weiss

Iron availability plays a decisive role in host-pathogen interaction, and limitation of iron availability to microbes has been characterized as an effective host defense strategy. The identification of the iron-scavenging property of the neutrophil protein calprotectin adds an important new piece to this concept of nutritional immunity.

Chemical ecology: Washing out worms

September 17th, 2015 by Catherine Goodman

Nature Chemical Biology 11, 754 (2015). doi:10.1038/nchembio.1922

Author: Catherine Goodman

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.