Volume 16 Issue 8, 1 August 2020

Rho family GTPases regulate cell behaviors through complex signaling networks that act on rapid timescales in subcellular spatial domains. New live-cell biosensors and analytical methods now provide critical tools to dissect Rho GTPase regulation and to better understand cellular information processing.

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.

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.

This Review discusses chemotype-specific mechanisms of drug resistance and chemical strategies to overcome resistance.

Biosensors of guanine exchange factors (GEFs) and red-shifted GTPase biosensors are used to visualize GEF and GTPase activities in the same cells and enable correlation analysis to reveal which GEF–GTPase interactions regulate cell movement.

Structural and smFRET analysis reveals the mechanism of opposing catalytic activities of bifunctional Rel enzymes; that is, activation of one of the catalytic domains leads to allosteric inactivation of the other.

Development of BRET sensors for nearly all major G proteins show that GPCR–G-protein coupling ranges from promiscuous to extremely specific, Switch III is a novel site for G-protein engineering, and optimal donor–acceptor positioning is non-obvious.

In plants, the cytosolic phenylalanine biosynthetic intermediate phenylpyruvate can serve as an amino acceptor in tryptophan-dependent auxin biosynthesis, thus facilitating crosstalk between these two distinct primary metabolic pathways.

Engineering of yeast transcription factors and design of hybrid DNA promoter elements have resulted in a toolkit for tunable and orthogonal regulation of gene expression in Arabidopsis thaliana and Nicotiana benthamiana plants.

Using a new method to generate site-specific monoubiquitinated proteins, the authors find monoubiquitination has a site-specific effect on protein stability and proteasomal processing.

Prostaglandins PGE1 and PGA1 have neuroprotective effects by enhancing the transcriptional activity of Nurr1 by directly binding to its ligand-binding domain and upregulating their target genes implicated in Parkinson’s disease.

The authors developed a metabolic labeling method via incorporation of allyl-SAM analogs to profile transcriptome-wide m⁶A at base resolution, which enables identification of m⁶A motifs and clustered m⁶A sites.

An antibody-independent m⁶A profiling method called m⁶A-SEAL was developed via turning m⁶A into stable dm⁶A after treatment by FTO and DTT. This method exhibits better reliability in detection of transcriptome-wide m⁶A sites in humans and plants.

Rather than a typical S-adenosylmethionine-dependent alkyltransferase, the installation of the N-alkylamine linker in several nucleoside antibiotics is catalyzed via γ-replacement by a pyridoxal-5′-phosphate-dependent aminobutyryltransferase.

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.

Comprehensive informatic, structural and biochemical characterization of the GH128 family defines subgroups of glycoside hydrolase enzymes with unique recognition and cleavage mechanisms for 1,3-beta-glucan polysaccharide substrates.