Zhixia Ye

MeSH headings : Acetyltransferases / chemistry; Acetyltransferases / genetics; Acetyltransferases / metabolism; Acyl Carrier Protein / chemistry; Acyl Carrier Protein / genetics; Acyl Carrier Protein / metabolism; Bacterial Proteins / chemistry; Bacterial Proteins / genetics; Bacterial Proteins / metabolism; Conserved Sequence; Cross-Linking Reagents; Escherichia coli / genetics; Escherichia coli / metabolism; Escherichia coli Proteins / chemistry; Escherichia coli Proteins / genetics; Escherichia coli Proteins / metabolism; Fatty Acid Synthase, Type II / chemistry; Fatty Acid Synthase, Type II / genetics; Fatty Acid Synthase, Type II / metabolism; Models, Molecular; Mutagenesis, Site-Directed; Open Reading Frames; Photochemical Processes; Protein Interaction Domains and Motifs; Saccharopolyspora / genetics; Saccharopolyspora / metabolism; Streptomyces coelicolor / genetics; Streptomyces coelicolor / metabolism

TL;DR: Unnatural amino acid mutagenesis is used to site specifically install photo-cross-linking functionality into acyl carrier proteins from diverse systems and the ketosynthase FabF from the Escherichia coli type II fatty acid synthase to demonstrate that unnatural amino acid based photo-Cross-l linking is a powerful tool for probing and interrogating protein interactions in complex biosynthetic systems. (via Semantic Scholar)

MeSH headings : Acyl Carrier Protein / metabolism; Acyl Coenzyme A / metabolism; Acyltransferases / metabolism; Molecular Structure; Pyridones / metabolism

TL;DR: An assay to probe ACP interactions based on leveraging the extender unit promiscuity of KirCII is developed and allows us to identify residues on the ACP surface that contribute to specific recognition by KirC II. (via Semantic Scholar)

MeSH headings : Acyl Carrier Protein / chemistry; Acyl Carrier Protein / metabolism; Codon, Terminator; Cross-Linking Reagents / chemistry; Cross-Linking Reagents / metabolism; Fatty Acid Synthases / chemistry; Fatty Acid Synthases / metabolism; Kinetics; Mutagenesis, Site-Directed; Polyketide Synthases / chemistry; Polyketide Synthases / metabolism; Polyketides / metabolism; Protein Conformation

TL;DR: This work reports a facile strategy for rapidly reporting such ACP-KS interactions based on the incorporation of an amino acid with photocrosslinking functionality that can be applied to any polyketide or fatty acid synthase regardless of substrate specificity. (via Semantic Scholar)