This study confirmed the participation of a cryptic palmitoyl fatty acyl chain in the biosynthesis of safracin and unraveled a previously ignored peptidase for the removal of the precursor. Furthermore, the post-assembly line tailoring steps are extensively studied in terms of the methyltransferase SacI-catalyzed N-methylation and the FAD-dependent monooxygenase SacJ-catalyzed A-ring oxidation. The timing of these post-NRPS steps is also addressed in this work.
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A Cryptic Palmitoyl Chain Involved in Safracin Biosynthesis Facilitates Post-NRPS Modifications.
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State Key Laboratory of Bioorganic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai 200032, China.
This study confirmed the participation of a cryptic palmitoyl fatty acyl chain in the biosynthesis of safracin and unraveled a previously ignored peptidase for the removal of the precursor. Furthermore, the post-assembly line tailoring steps are extensively studied in terms of the methyltransferase SacI-catalyzed N-methylation and the FAD-dependent monooxygenase SacJ-catalyzed A-ring oxidation. The timing of these post-NRPS steps is also addressed in this work.
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The posttranslational addition of palmitate to cysteines occurs ubiquitously in eukaryotic cells, where it functions in anchoring target proteins to membranes and in vesicular trafficking. Here we show that the Saccharomyces cerevisiae palmitoyltransferase Pfa4 enhanced heterochromatin formation at the cryptic mating-type loci HMR and HML via Rif1, a telomere regulatory protein. Acylated Rif1 was detected in extracts from wild-type but not pfa4Δ mutant cells.
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Division of Physiology and Pathophysiology, School of Pharmaceutical Sciences, Kinki University, 3-4-1 Kowakae, Higashi-Osaka 577-8502, Japan.
Proteinase-activated receptor-1 (PAR1), a G protein-coupled receptor (GPCR) for thrombin, can be activated not only by PAR1-activating peptides (PAR1APs) based on the N-terminal cryptic tethered ligand sequence but also by an N-palmitoylated (Pal) peptide, Pal-RCLSSSAVANRSKKSRALF-amide (P1pal-19), based on the intracellular loop 3 of PAR1, designated pepducin, in human platelets or PAR1-transfected cells. The present article evaluated the actions of P1pal-19 and also the shorter peptide, Pal-RCLSSSAVANRS-amide (P1pal-12), known as a possible PAR1 antagonist, in multiple cells/tissues that naturally express PAR1. P1pal-19 as well as a PAR1AP, TFLLR-amide, evoked cytosolic Ca(2+) mobilization in cultured human lung epithelial cells (A549) and rat gastric mucosal epithelial cells (RGM1).
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