中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Function of PsbO-Asp158 in photosystem II: effects of mutation of this residue on the binding of PsbO and function of PSII in Thermosynechococcus vulcanus

文献类型:期刊论文

作者Zhu, Qingjun3; Yang, Yanyan; Xiao, Yanan3; Wang, Wenda3; Kuang, Tingyun; Shen, Jian-Ren; Han, Guangye
刊名PHOTOSYNTHESIS RESEARCH
出版日期2020
卷号146期号:1-3页码:29-40
关键词PsbO Site-directed mutagenesis Photosystem II Oxygen evolution Thermosynechococcus vulcanus
ISSN号0166-8595
DOI10.1007/s11120-020-00715-0
文献子类Article
英文摘要PsbO-D158 is a highly conserved residue of the PsbO protein in photosystem II (PSII), and participates in one of the hydrogen-bonding networks connecting the manganese cluster with the lumenal surface. In order to examine the role of PsbO-D158, we mutated it to E, N or K in Thermosynechococcus vulcanus and characterized photosynthetic properties of the mutants obtained. The growth rates of these three mutants were similar to that of the wild type, whereas the oxygen-evolving activity of the three mutant cells decreased to 60-64% of the wild type. Fluorescence kinetics showed that the mutations did not affect the electron transfer from Q(A) to Q(B), but slightly affected the donor side of PSII. Moreover, all of the three mutant cells were more sensitive to high light and became slower to recover from photoinhibition. In the isolated thylakoid membranes from the three mutants, the PsbU subunit was lost and the oxygen-evolving activity was reduced to a lower level compared to that in the respective cells. PSII complexes isolated from these mutants showed no oxygen-evolving activity, which was found to be due to large or complete loss of PsbO, PsbV and PsbU during the process of purification. Moreover, PSII cores purified from the three mutants contained Psb27, an assembly co-factor of PSII. These results suggest that PsbO-D158 is required for the proper binding of the three extrinsic proteins to PSII and plays an important role in maintaining the optimal oxygen-evolving activity, and its mutation caused incomplete assembly of the PSII complex.
学科主题Plant Sciences
出版地DORDRECHT
电子版国际标准刊号1573-5079
WOS关键词MANGANESE-STABILIZING PROTEIN ; SITE-DIRECTED MUTANTS ; EXTRINSIC PROTEINS ; OXYGEN-EVOLUTION ; DELETION MUTAGENESIS ; WATER OXIDATION ; CLUSTER ; SUBUNIT ; POLYPEPTIDE ; ELONGATUS
WOS研究方向Plant Sciences
语种英语
WOS记录号WOS:000518147700001
出版者SPRINGER
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]
源URL[http://ir.ibcas.ac.cn/handle/2S10CLM1/21882]  
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.Univ Chinese Acad Sci, Yuquan Rd, Beijing 100049, Peoples R China
3.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
Zhu, Qingjun,Yang, Yanyan,Xiao, Yanan,et al. Function of PsbO-Asp158 in photosystem II: effects of mutation of this residue on the binding of PsbO and function of PSII in Thermosynechococcus vulcanus[J]. PHOTOSYNTHESIS RESEARCH,2020,146(1-3):29-40.
APA Zhu, Qingjun.,Yang, Yanyan.,Xiao, Yanan.,Wang, Wenda.,Kuang, Tingyun.,...&Han, Guangye.(2020).Function of PsbO-Asp158 in photosystem II: effects of mutation of this residue on the binding of PsbO and function of PSII in Thermosynechococcus vulcanus.PHOTOSYNTHESIS RESEARCH,146(1-3),29-40.
MLA Zhu, Qingjun,et al."Function of PsbO-Asp158 in photosystem II: effects of mutation of this residue on the binding of PsbO and function of PSII in Thermosynechococcus vulcanus".PHOTOSYNTHESIS RESEARCH 146.1-3(2020):29-40.

入库方式: OAI收割

来源:植物研究所

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