| Literature DB >> 29106068 |
Chao Xue1, Shuai Liu1, Chen Chen1, Jun Zhu2, Xibin Yang2, Yong Zhou1, Rui Guo1, Xiaoyu Liu1, Zhiyun Gong1.
Abstract
Lysine acetylation (Kac) is an important protein post-translational modification in both eukaryotes and prokaryotes. Herein, we report the results of a global proteome analysis of Kac and its diverse functions in rice (Oryza sativa). We identified 1353 Kac sites in 866 proteins in rice seedlings. A total of 11 Kac motifs are conserved, and 45% of the identified proteins are localized to the chloroplast. Among all acetylated proteins, 38 Kac sites are combined in core histones. Bioinformatics analysis revealed that Kac occurs on a diverse range of proteins involved in a wide variety of biological processes, especially photosynthesis. Protein-protein interaction networks of the identified proteins provided further evidence that Kac contributes to a wide range of regulatory functions. Furthermore, we demonstrated that the acetylation level of histone H3 (lysine 27 and 36) is increased in response to cold stress. In summary, our approach comprehensively profiles the regulatory roles of Kac in the growth and development of rice.Entities:
Keywords: Oryza sativa; acetylome; cold stress; lysine acetylation; photosynthesis
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Year: 2018 PMID: 29106068 DOI: 10.1002/pmic.201700036
Source DB: PubMed Journal: Proteomics ISSN: 1615-9853 Impact factor: 3.984