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Enzymes of cysteine synthesis show extensive and conserved modifications patterns that include N(α)-terminal acetylation.
Amino Acids 2010; 39(4):1077-86AA

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 not only to a high reproducibility of SAP but likely biological significance of each subspecies. The most abundant OAS-TL subspecies in cytosol and plastids were subject of N-terminal processing followed by acetylation of the newly originated N-terminus. The mode of N(α)-terminal acetylation of OAS-TL and its possible biological function are discussed.

Authors+Show Affiliations

Heidelberg Institute for Plant Sciences, University of Heidelberg, Germany.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

20658158

Citation

Wirtz, Markus, et al. "Enzymes of Cysteine Synthesis Show Extensive and Conserved Modifications Patterns That Include N(α)-terminal Acetylation." Amino Acids, vol. 39, no. 4, 2010, pp. 1077-86.
Wirtz M, Heeg C, Samami AA, et al. Enzymes of cysteine synthesis show extensive and conserved modifications patterns that include N(α)-terminal acetylation. Amino Acids. 2010;39(4):1077-86.
Wirtz, M., Heeg, C., Samami, A. A., Ruppert, T., & Hell, R. (2010). Enzymes of cysteine synthesis show extensive and conserved modifications patterns that include N(α)-terminal acetylation. Amino Acids, 39(4), pp. 1077-86. doi:10.1007/s00726-010-0694-0.
Wirtz M, et al. Enzymes of Cysteine Synthesis Show Extensive and Conserved Modifications Patterns That Include N(α)-terminal Acetylation. Amino Acids. 2010;39(4):1077-86. PubMed PMID: 20658158.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Enzymes of cysteine synthesis show extensive and conserved modifications patterns that include N(α)-terminal acetylation. AU - Wirtz,Markus, AU - Heeg,Corinna, AU - Samami,Arman Allboje, AU - Ruppert,Thomas, AU - Hell,Rüdiger, Y1 - 2010/07/24/ PY - 2010/03/03/received PY - 2010/07/09/accepted PY - 2010/7/27/entrez PY - 2010/7/27/pubmed PY - 2010/12/14/medline SP - 1077 EP - 86 JF - Amino acids JO - Amino Acids VL - 39 IS - 4 N2 - 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 not only to a high reproducibility of SAP but likely biological significance of each subspecies. The most abundant OAS-TL subspecies in cytosol and plastids were subject of N-terminal processing followed by acetylation of the newly originated N-terminus. The mode of N(α)-terminal acetylation of OAS-TL and its possible biological function are discussed. SN - 1438-2199 UR - https://www.unboundmedicine.com/medline/citation/20658158/Enzymes_of_cysteine_synthesis_show_extensive_and_conserved_modifications_patterns_that_include_N_α__terminal_acetylation_ L2 - https://dx.doi.org/10.1007/s00726-010-0694-0 DB - PRIME DP - Unbound Medicine ER -