Quantitative acetyl-proteome profiling of Camellia sinensis cv.‘Anji Baicha’ during periodic albinism reveal lysine acetylation of proteins involved in photosynthesis and secondary metabolite biosynthetic pathways

ABSTRACT: The tea plant (Camellia sinensis (L.) O. Kuntze) is often commercially used as a source of non-alcoholic beverages and is an economically important woody crop (Chen et al., 2007). As living standards have improved, the requirement for high-quality life has increased in modern society. ‘Anji Baicha’ (alias ‘Baiye 1’ or ‘White Leaf 1’) is an excellent tea cultivar with albino phenotype and it is popular in producing high-quality green tea. The traits of ‘Anji Baicha’ are as follows. Young ‘Anji Baicha’ shoots are yellow-green when the early spring temperature is below 20°C. As the leaves fully expand, the leaves become white. The leaves gradually return to green when the environmental temperature increases (Cheng et al., 1999; Li et al., 2002, 2011). Previous reports have suggested a positive correlation between amino acid concentration and albinism as well as a negative correlation between tea polyphenols and albinism (Li et al., 1996; Du et al., 2006; Xiong et al., 2013). Therefore, the quality of ‘Anji Baicha’ is much higher when new shoots become albino due to their rich amino acid content and modest tea polyphenol content. Plants adjust their metabolism in response to environmental stimuli to eventually bring about changes in protein activities and levels, and this adaptive process includes posttranslational protein modifications (PTMs) (Prabakaran et al., 2012). PTMs have been reported to regulate various processes, including DNA interaction, protein-protein interactions, enzyme activation and protein stability. Among the hundreds of different PTMs, lysine acetylation is an abundant, reversible and highly regulated PTM (Zhang et al., 2009; Wu et al., 2011).

INSTRUMENT(S): Q Exactive

ORGANISM(S): Camellia Sinensis

TISSUE(S): Leaf

SUBMITTER: Rachel Green  

LAB HEAD: liang chen

PROVIDER: PXD008134 | Pride | 2018-01-15

REPOSITORIES: Pride