title: Mutational analysis of O-acetylserine (thiol) lyase conducted in yeast two-hybrid system.
abstract: Cysteine biosynthesis, achieved by the sequential reaction of two enzymes, serine acetyltransferase and O-acetylserine (thiol) lyase (OASTL), represents the final step of sulfur assimilation pathway in plants and bacteria. The two enzymes form a bi-enzymatic cysteine synthase complex through specific protein-protein interactions. To identify the amino acids important for cysteine synthase complex formation, several mutations in bacterial OASTL were designed. Effects of mutagenesis were verified in a yeast two-hybrid model that allowed monitoring both, protein-protein interactions and the enzymatic activity of OASTL.
authors.affiliation: Institute of Biochemistry and Biophysics, Polish Academy of Sciences, ul Pawińskiego 5A, Warsaw, Poland.
authors.forename: Frantz
authors.initials: F
authors.lastname: Liszewska
authors.forename: Małgorzata
authors.initials: M
authors.lastname: Lewandowska
authors.forename: Danuta
authors.initials: D
authors.lastname: Płochocka
authors.forename: Agnieszka
authors.initials: A
authors.lastname: Sirko
mesh_terms: D019757:Carbon-Oxygen Lyases / Q000235:genetics* / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics; D020798:Two-Hybrid System Techniques
chemical_list: C018725:O-acetylhomoserine (thiol)-lyase; D019757:Carbon-Oxygen Lyases