Structural insight into the formation of lipoprotein-β-barrel complexes
June 22nd, 2020 by Raquel Rodríguez-Alonso
Nature Chemical Biology, Published online: 22 June 2020; doi:10.1038/s41589-020-0575-0
A structural and biochemical study of bacterial β-barrel assembly machinery component BamA with transport substrate RcsF shows an inward-open conformation with RcsF trapped inside the β-barrel lumen and suggests a push–pull substrate export mechanism.Dissecting the Pol II transcription cycle and derailing cancer with CDK inhibitors
June 22nd, 2020 by Pabitra K. Parua
Nature Chemical Biology, Published online: 22 June 2020; doi:10.1038/s41589-020-0563-4
This Review provides insights into transcriptional regulation, and vulnerabilities of cancer cells to disruption of cyclin-dependent kinase (CDK)-mediated regulation of Pol II transcription, revealed with small-molecule CDK inhibitors.Groovy RNA polymerase
June 22nd, 2020 by Mirella Bucci
Nature Chemical Biology, Published online: 22 June 2020; doi:10.1038/s41589-020-0582-1
Groovy RNA polymeraseEnzymes knuckle down to the job
June 17th, 2020 by Paul H. Walton
Nature Chemical Biology, Published online: 17 June 2020; doi:10.1038/s41589-020-0585-y
A suite of new enzymes reveals more on how Nature breaks down plant-based polysaccharides and how these enzymes might be harnessed in the utilization of plant-based biomass.Viperin: an ancient radical-SAM enzyme finds its place in modern cellular metabolism and innate immunity [Immunology]
June 16th, 2020 by Soumi Ghosh, E. Neil G. Marsh
Viperin plays an important and multifaceted role in the innate immune response to viral infection. Viperin is also notable as one of very few radical SAM-dependent enzymes present in higher animals; however, the enzyme appears broadly conserved across all kingdoms of life, which suggests that it represents an ancient defense mechanism against viral infections. Although viperin was discovered some 20 years ago, only recently was the enzyme’s structure determined and its catalytic activity elucidated. The enzyme converts CTP to 3’,4’-didehydro-3’-deoxy-CTP, which functions as novel chain-terminating antiviral nucleotide when misincorporated by viral RNA-dependent RNA polymerases. Moreover, in higher animals, viperin interacts with numerous other host and viral proteins, and it is apparent that this complex network of interactions constitutes another important aspect of the protein’s antiviral activity. An emerging theme is that viperin appears to facilitate ubiquitin-dependent proteasomal degradation of some of the proteins it interacts with. Viperin- targeted protein degradation contributes to the antiviral response either by down-regulating various metabolic pathways important for viral replication or by directly targeting viral proteins for degradation. Here, we review recent advances in our understanding of the structure and catalytic activity of viperin, together with studies investigating the interactions between viperin and its target proteins. These studies have provided detailed insights into the biochemical processes underpinning this unusual enzyme’s wide-ranging antiviral activity. We also highlight recent intriguing reports that implicate a broader role for viperin in regulating non-pathological cellular processes, including thermogenesis and protein secretion.In vitro prototyping and rapid optimization of biosynthetic enzymes for cell design
June 15th, 2020 by Ashty S. Karim
Nature Chemical Biology, Published online: 15 June 2020; doi:10.1038/s41589-020-0559-0
The iPROBE platform accelerates the design and optimization of engineered biosynthetic pathways using a combination of cell-free protein synthesis, in vitro pathway assembly and a scoring system to identify high-performing combinations.Single-molecule analysis reveals agonist-specific dimer formation of µ-opioid receptors
June 15th, 2020 by Jan Möller
Nature Chemical Biology, Published online: 15 June 2020; doi:10.1038/s41589-020-0566-1
Single-molecule and super-resolution approaches define a monomer–dimer equilibrium of µ-opioid receptors and show that receptors form agonist-induced dimers coincident with β-arrestin2 binding to receptors.Unraveling proteasome engagement
June 15th, 2020 by Cameron G. Roberts
Nature Chemical Biology, Published online: 15 June 2020; doi:10.1038/s41589-020-0573-2
A new study reveals that, in addition to its longstanding role in recruiting proteins to the proteasome, ubiquitination can also induce a structural destabilization that allows the target protein to be efficiently unraveled for degradation.Author Correction: Higher-order epistasis shapes the fitness landscape of a xenobiotic-degrading enzyme
June 12th, 2020 by Gloria Yang
Nature Chemical Biology, Published online: 12 June 2020; doi:10.1038/s41589-020-0588-8
Author Correction: Higher-order epistasis shapes the fitness landscape of a xenobiotic-degrading enzyme[ASAP] Residue-Specific Binding Mechanisms of Thioflavin T to a Surface of Flat ß-Sheets within a Peptide Self-Assembly Mimic
June 9th, 2020 by
