Effects of Phosphorylation of beta Subunits of Phycocyanins on State Transition in the Model Cyanobacterium Synechocystis sp PCC 6803
Chen, Zhuo1; Zhan, Jiao1,2; Chen, Ying1; Yang, Mingkun1; He, Chenliu1; Ge, Feng1; Wang, Qiang1
刊名PLANT AND CELL PHYSIOLOGY
2015-10-01
卷号56期号:10页码:1997-2013
关键词beta subunits of phycocyanins (CpcBs) Phosphoproteomics Photosynthesis State transition Synechocystis sp PCC 6803 TiO2 enrichment
ISSN号0032-0781
英文摘要Synechocystis sp. PCC 6803 (hereafter Synechocystis) is a model cyanobacterium and has been used extensively for studies concerned with photosynthesis and environmental adaptation. Although dozens of protein kinases and phosphatases with specificity for Ser/Thr/Tyr residues have been predicted, only a few substrate proteins are known in Synechocystis. In this study, we report 194 in vivo phosphorylation sites from 149 proteins in Synechocystis, which were identified using a combination of peptide pre-fractionation, TiO2 enrichment and liquid chromatograpy-tandem mass spectrometry (LC-MS/MS) analysis. These phosphorylated proteins are implicated in diverse biological processes, such as photosynthesis. Among all identified phosphoproteins involved in photosynthesis, the beta subunits of phycocyanins (CpcBs) were found to be phosphorylated on Ser22, Ser49, Thr94 and Ser154. Four non-phosphorylated mutants were constructed by using site-directed mutagenesis. The in vivo characterization of the cpcB mutants showed a slower growth under high light irradiance and displayed fluorescence quenching to a lower level and less efficient energy transfer inside the phycobilisome (PBS). Notably, the non-phosphorylated mutants exhibited a slower state transition than the wild type. The current results demonstrated that the phosphorylation status of CpcBs affects the energy transfer and state transition of photosynthesis in Synechocystis. This study provides novel insights into the molecular mechanisms of protein phosphorylation in the regulation of photosynthesis in cyanobacteria and may facilitate the elucidation of the entire regulatory network by linking kinases to their physiological substrates.
WOS标题词Science & Technology ; Life Sciences & Biomedicine
类目[WOS]Plant Sciences ; Cell Biology
研究领域[WOS]Plant Sciences ; Cell Biology
关键词[WOS]SERINE/THREONINE PROTEIN-KINASES ; SP STRAIN PCC-6803 ; EXCITATION-ENERGY TRANSFER ; GRAM-NEGATIVE BACTERIUM ; PHOTOSYSTEM-I ; BACILLUS-SUBTILIS ; MYCOBACTERIUM-TUBERCULOSIS ; PHOSPHOPROTEOMIC ANALYSIS ; INTERACTION NETWORKS ; BLUE-GREEN
收录类别SCI
语种英语
WOS记录号WOS:000364961600011
内容类型期刊论文
源URL[http://ir.ihb.ac.cn/handle/342005/27364]  
专题水生生物研究所_水生生物分子与细胞生物学研究中心_期刊论文
作者单位1.Chinese Acad Sci, Inst Hydrobiol, Key Lab Algal Biol, Wuhan 430072, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100094, Peoples R China
推荐引用方式
GB/T 7714
Chen, Zhuo,Zhan, Jiao,Chen, Ying,et al. Effects of Phosphorylation of beta Subunits of Phycocyanins on State Transition in the Model Cyanobacterium Synechocystis sp PCC 6803[J]. PLANT AND CELL PHYSIOLOGY,2015,56(10):1997-2013.
APA Chen, Zhuo.,Zhan, Jiao.,Chen, Ying.,Yang, Mingkun.,He, Chenliu.,...&Wang, Qiang.(2015).Effects of Phosphorylation of beta Subunits of Phycocyanins on State Transition in the Model Cyanobacterium Synechocystis sp PCC 6803.PLANT AND CELL PHYSIOLOGY,56(10),1997-2013.
MLA Chen, Zhuo,et al."Effects of Phosphorylation of beta Subunits of Phycocyanins on State Transition in the Model Cyanobacterium Synechocystis sp PCC 6803".PLANT AND CELL PHYSIOLOGY 56.10(2015):1997-2013.
个性服务
查看访问统计
相关权益政策
暂无数据
收藏/分享
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。


©版权所有 ©2017 CSpace - Powered by CSpace