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

Amino Acids
Markus WirtzRüdiger Hell

Abstract

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 was shown to be crucial for efficient cysteine synthesis in Arabidopsis thaliana. In this study, the abundances of OAS-TLs were quantified independently by immunological detection in crude protein extracts and by SAT affinity purification (SAP) of OAS-TL. OAS-TL A and B were evidenced to be the most abundant isoforms in all analyzed tissues, which is consistent with micro array-based transcript analyses. Application of SAP to Arabidopsis revealed significant modification of the major OAS-TL isoforms present in cytosol, plastids and mitochondria into up to seven subspecies. Specific OAS-TL isoforms were found to be differentially modified in the leaves, roots, stem and cell culture. Sulphur deficiency did not alter modification of OAS-TL proteins purified from cell culture that showed the highest complexity of OAS-TL modifications. However, the pattern of OAS-TL modification was found to be stable within an analyzed tissue, pointing no...Continue Reading

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Citations

Jun 26, 2012·The Journal of Biological Chemistry·Markus WirtzRüdiger Hell
Nov 29, 2013·Molecular Plant·Luis C RomeroCecilia Gotor
Nov 29, 2017·Journal of Plant Research·Md Harun-Ur- RashidHirosuke Oku
Mar 4, 2021·Nature Communications·Sheng-Kai SunFang-Jie Zhao

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