Mutational analysis of O-acetylserine (thiol) lyase conducted in yeast two-hybrid system.
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.
Liszewska
Frantz
F
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, ul Pawińskiego 5A, Warsaw, Poland.
Lewandowska
Małgorzata
M
Płochocka
Danuta
D
Sirko
Agnieszka
A
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
C018725:O-acetylhomoserine (thiol)-lyase; D019757:Carbon-Oxygen Lyases