Plant Molecular Biology

, Volume 99, Issue 1–2, pp 123–134 | Cite as

Characterization of the O-acetylserine(thiol)lyase gene family in Solanum lycopersicum L.

  • Danmei Liu
  • Juanjuan Lu
  • Hui Li
  • Juanjuan Wang
  • Yanxi PeiEmail author


Key message

This research demonstrated the conservation and diversification of the functions of the O-acetylserine-(thiol) lyase gene family genes in Solanum lycopersicum L.


Cysteine is the first sulfur-containing organic molecule generated by plants and is the precursor of many important biomolecules and defense compounds. Cysteine and its derivatives are also essential in various redox signaling-related processes. O-acetylserine(thiol)lyase (OASTL) proteins catalyze the last step of cysteine biosynthesis. Previously, researches focused mainly on OASTL proteins which were the most abundant or possessed the authentic OASTL activity, whereas few studies have ever given a comprehensive view of the functions of all the OASTL members in one specific species. Here, we characterized 8 genes belonging to the OASTL gene family from tomato genome (SlOAS2 to SlOAS9), including the sequence analyses, subcellular localization, enzymatic activity assays, expression patterns, as well as the interaction property with SATs. Apart from SlOAS3, all the other genes encoded OASTL-like proteins. Tomato OASTLs were differentially expressed during the development of tomato plants, and their encoded proteins had diverse compartmental distributions and functions. SlOAS5 and SlOAS6 catalyzed the biogenesis of cysteine in chloroplasts and in the cytosol, respectively, and this was in consistent with their interaction abilities with SlSATs. SlOAS4 catalyzed the generation of hydrogen sulfide, similar to its Arabidopsis ortholog, DES1. SlOAS2 also functioned as an L-cysteine desulfhydrase, but its expression pattern was very different from that of SlOAS4. Additionally, SlOAS8 might be a β-cyanoalanine synthase in mitochondria, and the S-sulfocysteine synthase activity appeared lost in tomato plants. SlOAS7 exhibited a transactivational ability in yeast; while the subcellular localization of SlOAS9 was in the peroxisome and correlated with the process of leaf senescence, indicating that these two genes might have novel roles.


Tomato OASTL SAT Enzymatic activity Subcellular localization Expression pattern 



This work is funded by the National Natural Science Foundation of China (31501772) and Shanxi Province Science Foundation for Youths (201601D021097). We thank Dr. Yongfu Fu for tomato seeds of cv. MicroTom and the vector pGWB555. We thank Drs. Lifang Niu, Zhengrui Qin and Liyu Huang for providing the subcellular localization vectors. We thank International Science Editing ( for editing this manuscript.

Author contribution

DL and YP conceived the project and designed experiments; DL, JL, HL, JW performed experiments; DL and YP analysed experiment data and wrote the manuscript.

Supplementary material

11103_2018_807_MOESM1_ESM.pdf (838 kb)
Supplementary material 1 (PDF 837 KB)


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Copyright information

© Springer Nature B.V. 2018

Authors and Affiliations

  1. 1.College of Life ScienceShanxi UniversityTaiyuanChina
  2. 2.Scientific Instrument CenterShanxi UniversityTaiyuanChina

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