Enzymes of cysteine synthesis show extensive and conserved modifications patterns that include N(α)-terminal acetylation

• Published in: Amino acids Vol. 39; no. 4; p. 1077
• Main Authors: Wirtz, Markus, Heeg, Corinna, Samami, Arman Allboje, Ruppert, Thomas, Hell, Rüdiger
• Format: Journal Article
• Language: English
• Published: Austria 01.10.2010
• Subjects: Acetylation; Arabidopsis - enzymology; Arabidopsis - genetics; Arabidopsis - metabolism; Arabidopsis Proteins - genetics; Arabidopsis Proteins - metabolism; Cysteine - biosynthesis; Cysteine Synthase - chemistry; Cysteine Synthase - genetics; Cysteine Synthase - isolation & purification; Cysteine Synthase - metabolism; Cytosol - enzymology; Electrophoresis, Polyacrylamide Gel; Gene Expression Regulation, Plant; Isoenzymes - chemistry; Isoenzymes - genetics; Isoenzymes - isolation & purification; Isoenzymes - metabolism; Mass Spectrometry; Mitochondria - enzymology; Plant Leaves - enzymology; Plant Leaves - genetics; Plant Leaves - metabolism; Plant Roots - enzymology; Plant Stems - enzymology; Plastids - enzymology; Protein Processing, Post-Translational; Sequence Analysis, Protein; Serine O-Acetyltransferase - metabolism; Sulfhydryl Compounds - metabolism; Sulfur - metabolism

Biosynthesis of cysteine is a two-step process in higher plants subsequently catalyzed by serine acetyltransferase (SAT) and O-acetylserine (thiol) lyase (OAS-TL) which are present in cytosol, plastids and mitochondria. Recently, the distribution of SAT and OAS-TL in these subcellular compartments w...