title: An engineered lantipeptide synthetase serves as a general leader peptide-dependent kinase.
abstract: Phosphorylation is an abundant post-translational modification involved in a myriad of cell signaling pathways. Herein, we have engineered the class II lantipeptide synthetase ProcM to generate a variety of peptides containing O-phosphoserine (pSer) and O-phosphothreonine (pThr) residues, either in vitro or in vivo.
authors.affiliation: Department of Chemistry and Howard Hughes Medical Institute, University of Illinois at Urbana-Champaign, 600 S Mathews Ave, Urbana, IL 61801, USA.
authors.forename: Gabrielle N
authors.initials: GN
authors.lastname: Thibodeaux
authors.forename: Wilfred A
authors.initials: WA
authors.lastname: van der Donk
mesh_terms: D019943:Amino Acid Substitution; D010455:Peptides / Q000378:metabolism*; D010766:Phosphorylation; D010768:Phosphoserine / Q000737:chemistry; D010769:Phosphothreonine / Q000737:chemistry; D011499:Protein Processing, Post-Translational; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*; D021382:Protein Sorting Signals; D013379:Substrate Specificity
chemical_list: D010455:Peptides; D021382:Protein Sorting Signals; D010769:Phosphothreonine; D010768:Phosphoserine; D017346:Protein Serine-Threonine Kinases