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Reversible transcriptional repressors are built with TALE proteins on the basis of steric hindrance of a new promoter architecture in an RNA-sensitive manner, enabling applications in mammalian cells such as classification of cancerous versus noncancerous cells.
Membrane sorting of Ras and its isolated lipid anchor is based on membrane curvature, sensed by Ras itself. This helps to explain the previous inability to match in vivo results in vitro in promoting the raftophilic Ras to partition with membrane lipid rafts.
Inhibitors of the PAD4 enzyme that bind the inactive enzyme link this protein deiminase and the resultant arginine-to-citrulline modification to formation of neutrophil extracellular traps, highly decondensed chromatin structures with both host-defense and pathological roles.
The reliable identification of microRNA (miRNA) targets remains an elusive goal. A new technique, using specially modified synthetic miRNAs to directly capture bound RNAs, brings us closer.
Lysophosphatidylserines (lyso-PSs) are an emerging class of signaling lipids implicated in human inflammatory and autoimmune diseases. A newly discovered phosphatidylserine-specific lipase, ABHD16A, together with the recently described lyso-PS lipase ABHD12 shed light on the in vivo regulation of lyso-PS, providing a potential enzymatic target for modulating neuroinflammatory responses.
An international group of chemical biologists convened in San Francisco to present the latest scientific findings, discuss future directions and be inspired by research at the interface of chemistry and biology. This report on the third annual conference of the International Chemical Biology Society provides a brief overview of the meeting and its scientific program.
The natural product albicidin is known to be a potential antibacterial agent, but its missing structure has stymied further studies. Structural determination and biochemical tests of NRPS domains now identify an unusual p-aminobenzoic acid–based compound.
The construction of ClpX hexamers containing variable numbers and configurations of wild-type and grip-defective pore loops supports a model of concurrent loop movement that ensures substrate unfolding and translocation.
Recent studies on two enzyme classes operating at the membrane interface showcase an unanticipated degree of structural plasticity involving domain swapping and marked secondary structure reshuffling. This structural variability in topology is key to functional diversification and catalytic prowess.
ABHD16A is identified as a major enzyme catalyzing production of lyso-PS from phosphatidylserine (PS). A new ABHD16A inhibitor and knockout mice show a dynamic interplay occurring during inflammation between ABHD16A and disease-linked ABHD12, an enzyme that degrades lyso-PS.