Role of PsbV-Tyr137 in photosystem II studied by site-directed mutagenesis in the thermophilic cyanobacterium Thermosynechococcus vulcanus
Xiao, Yanan4; Zhu, Qingjun4; Yang, Yanyan; Wang, Wenda; Kuang, Tingyun; Shen, Jian-Ren; Han, Guangye
刊名PHOTOSYNTHESIS RESEARCH
2020
卷号146期号:1-3页码:41-54
关键词Photosystem II Extrinsic proteins PsbV Hydrogen-bond network Site-directed mutagenesis Water-splitting
ISSN号0166-8595
DOI10.1007/s11120-020-00753-8
文献子类Article
英文摘要PsbV (cytochrome c(550)) is one of the three extrinsic proteins of photosystem II (PSII) and functions to maintain the stability and activity of the Mn4CaO5 cluster, the catalytic center for water oxidation. PsbV-Y137 is the C-terminal residue of PsbV and is located at the exit of a hydrogen-bond network mediated by the D1-Y161-H190 residue pair. In order to examine the function of PsbV-Y137, four mutants, PsbV-Y137A, PsbV-Y137F, PsbV-Y137G, and PsbV-Y137W, were generated with Thermosynechococcus vulcanus (T. vulcanus). These mutants showed growth rates similar to that of the wild-type strain (WT); however, their oxygen-evolving activities were different. At pH 6.5, the oxygen evolution rates of Y137F and Y137W were almost identical to that of WT, whereas the oxygen evolution rates of the Y137A, Y137G mutants were 64% and 61% of WT, respectively. However, the oxygen evolution in the latter two mutants decreased less at higher pHs, suggesting that higher pHs facilitated oxygen evolution probably by facilitating proton egress in these two mutants. Furthermore, thylakoid membranes isolated from the PsbV-Y137A, PsbV-Y137G mutants exhibited much lower levels of oxygen-evolving activity than that of WT, which was found to be caused by the release of PsbV. In addition, PSII complexes purified from the PsbV-Y137A and PsbV-Y137G mutants lost all of the three extrinsic proteins but instead bind Psb27, an assembly cofactor of PSII. These results demonstrate that the PsbV-Tyr137 residue is required for the stable binding of PsbV to PSII, and the hydrogen-bond network mediated by D1-Y161-H190 is likely to function in proton egress during water oxidation.
学科主题Plant Sciences
电子版国际标准刊号1573-5079
出版地DORDRECHT
WOS关键词EXTRINSIC PROTEINS ; CYTOCHROME C-550 ; FUNCTIONAL-PROPERTIES ; CHLOROPHYLL FLUORESCENCE ; CYANIDIUM-CALDARIUM ; MANGANESE CLUSTER ; CRYSTAL-STRUCTURE ; WATER OXIDATION ; 12-KDA PROTEIN ; RED ALGA
WOS研究方向Plant Sciences
语种英语
出版者SPRINGER
WOS记录号WOS:000529115500001
资助机构National Key R&D Program of China [2017YFA0503700] ; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31470339] ; Strategic Priority Research Program of CAS [XDB17000000] ; Key Research Program of Frontier Sciences, CAS [QYZDY-SSW-SMC003]
内容类型期刊论文
源URL[http://ir.ibcas.ac.cn/handle/2S10CLM1/21785]  
专题中科院光生物学重点实验室
作者单位1.Okayama Univ, Res Inst Interdisciplinary Sci, Grad Sch Nat Sci & Technol, Tsushima Naka 3-1-1, Okayama 7008530, Japan
2.Chinese Acad Sci, Innovat Acad Seed Design, 1 Beichen West Rd, Beijing 100101, Peoples R China
3.Univ Chinese Acad Sci, Yuquan Rd, Beijing 100049, Peoples R China
4.Chinese Acad Sci, Photosynth Res Ctr, Key Lab Photobiol, Inst Bot, 20 Nanxincun, Beijing 100093, Peoples R China
推荐引用方式
GB/T 7714
Xiao, Yanan,Zhu, Qingjun,Yang, Yanyan,et al. Role of PsbV-Tyr137 in photosystem II studied by site-directed mutagenesis in the thermophilic cyanobacterium Thermosynechococcus vulcanus[J]. PHOTOSYNTHESIS RESEARCH,2020,146(1-3):41-54.
APA Xiao, Yanan.,Zhu, Qingjun.,Yang, Yanyan.,Wang, Wenda.,Kuang, Tingyun.,...&Han, Guangye.(2020).Role of PsbV-Tyr137 in photosystem II studied by site-directed mutagenesis in the thermophilic cyanobacterium Thermosynechococcus vulcanus.PHOTOSYNTHESIS RESEARCH,146(1-3),41-54.
MLA Xiao, Yanan,et al."Role of PsbV-Tyr137 in photosystem II studied by site-directed mutagenesis in the thermophilic cyanobacterium Thermosynechococcus vulcanus".PHOTOSYNTHESIS RESEARCH 146.1-3(2020):41-54.
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