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Shown is the tropical greenhouse of the Matthaei Botanical Gardens. Plants from botanical collections at the University of Michigan have been used for the bioinformatic discovery of plant peptides with new side-chain macrocyclizations derived from a copper-dependent autocatalytic peptide cyclase called the BURP domain.
An autocatalytic peptide cyclase defines a new subclass of plant ribosomally synthesized and post-translationally modified peptides (RiPPs). This discovery explains the origins of a large family of cyclic peptides and inspires new tools for mining these RiPPs across the plant kingdom.
Genetic code expansion is emerging as a promising strategy to precisely regulate protein expression. A new study engineered cells that enabled noncanonical-amino-acid-triggered insulin expression to rapidly regulate blood glucose levels in a diabetic mouse model.
The molecular mechanism through which chromatin-bound RNA-binding proteins (chrRBPs) control transcription remains obscure. A new study reveals that chrRBPs can compartmentalize RNA and transcription machinery into a phase-separated condensate, thus modulating gene expression.
A new study demonstrates that the receptor-binding domain of the SARS-CoV-2 spike protein binds to sialylated glycans, especially glycolipids, to facilitate viral entry, an insight that identifies new potential targets for SARS-CoV-2 interventions.
The diversity of biological pathways that are regulated by protein post-translational modification with O-GlcNAc requires community engagement to develop and apply tools to probe the biological and disease-relevant functions of these modifications.
BURP domains within lyciumin precursor peptides serve as autocatalytic peptide cyclases, enabling the discovery of other BURP-domain-derived products and development of a bioinformatic method to mine plants for precursor-peptide-encoding genes.
An approach relying on guide RNA pairs encoding the same edits in both sense and antisense DNA strands is developed to improve the editing capability of prime editing in human cells.
CRISPR–Cas9 genome editing is limited in organisms with inefficient homology-directed repair (HDR), but development of a specialized CRISPR platform conferred increased HDR rates in four noncanonical yeasts to enhance strain engineering.
The development of a genetic code expansion-based system enables fast protein expression in response to a noncanonical amino acid. The system was implanted into diabetic mice to rescue hyperglycemia with oral delivery of the amino acid.
Discovery of a chemical probe targeting the PWWP domain of NSD2 reveals insight into mechanisms that govern NSD2 localization. The compound and its negative control represent valuable tools for further defining NSD2 biology.
The agrochemical mandipropamid (Mandi), which induces dimerization of a variant of the abscisic acid receptor, has been developed as a new chemical inducer of proximity for cellular and organismal applications.
With the example of the paraspeckle protein PSPC1, Shao et al. demonstrated the synergistic interplay of promoter-associated RNA and its binding proteins in promoting transcription condensate formation and Pol II engagement and activity via phase separation.
Mass spectrometric profiling of a glycan library reveals that sialylated glycans, especially sialic acid-containing gangliosides, interact with the RBD of the SARS-CoV-2 spike protein and are involved in ACE2-dependent viral infection.
Biochemical and structural characterization of a homozygous point mutation in the GPX4 gene (R152H) reveals loss of enzymatic function and resistance to degradation. Therapeutic treatments such as selective antioxidants can overcome R152H defects.
Structures of the bifunctional heme transporter cytochrome c synthase CcsBA in closed and open states show how heme binding in the periplasmic site induces a conformational shift, exposing the heme and facilitating its transfer to apocytochrome c.
Determination of the cryo-EM structures of active neurokinin-1 receptor bound to substance P or the Gq biased peptide SP6–11 reveals that interactions with the receptor extracellular loops regulate G protein signaling selectivity.