作者: Xin Liu , Mingkun Yang , Yan Wang , Zhuo Chen , Jia Zhang
DOI: 10.1093/PCP/PCY080
关键词: Photosynthesis 、 Biochemistry 、 Cyanobacteria 、 Synechococcus 、 Metabolism 、 Succinylation 、 Protein succinylation 、 Chemistry 、 Photosynthetic efficiency 、 Photosynthetic reaction centre
摘要: Lysine succinylation is a newly identified protein post-translational modification and plays important roles in various biological pathways both prokaryotes eukaryotes, but its extent function photosynthetic organisms remain largely unknown. Here, we performed the first systematic studies of lysine cyanobacteria, which are only capable oxygenic photosynthesis established model for studying mechanisms. By using mass spectrometry analysis combination with enrichment succinylated peptides from digested cell lysates, 1,704 sites on 691 proteins cyanobacterium Synechococcus sp. PCC 7002. Bioinformatic revealed that large proportion were present metabolism. Among all involved photosynthesis, PSII manganese-stabilizing (PsbO) was found to be Lys99 Lys234. Functional PsbO by site-directed mutagenesis, mutants mimicking either constitutively (K99E K234E) or non-succinylated states (K99R K234R) constructed. The succinylation-mimicking K234E mutant exhibited decreased oxygen evolution rate center efficiency energy transfer during reaction. Molecular dynamics simulations suggested mechanism may allow influence altering conformation PsbO, thereby hindering interaction between core. Our findings suggest reversible an regulatory Synechococcus, as well other organisms.