NdhV subunit regulates the activity of type-1 NAD(P)H dehydrogenase under high light conditions in cyanobacterium Synechocystis sp PCC 6803

doi:10.1038/srep28361

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	NdhV subunit regulates the activity of type-1 NAD(P)H dehydrogenase under high light conditions in cyanobacterium Synechocystis sp PCC 6803
	Chen, Xin 3; He, Zhihui ; Xu, Min ; Peng, Lianwei 1; Mi, Hualing
刊名	SCIENTIFIC REPORTS
	2016
卷号	6
ISSN号	2045-2322
DOI	10.1038/srep28361
文献子类	Article
英文摘要	The cyanobacterial NAD(P)H dehydrogenase (NDH-1) complexes play crucial roles in variety of bioenergetic reactions. However, the regulative mechanism of NDH-1 under stressed conditions is still unclear. In this study, we detected that the NDH-1 activity is partially impaired, but the accumulation of NDH-1 complexes was little affected in the NdhV deleted mutant (Delta ndhV) at low light in cyanobacterium Synechocystis sp. PCC 6803. Delta ndhV grew normally at low light but slowly at high light under inorganic carbon limitation conditions (low pH or low CO2), meanwhile the activity of CO2 uptake was evidently lowered than wild type even at pH 8.0. The accumulation of NdhV in thylakoids strictly relies on the presence of the hydrophilic subcomplex of NDH-1. Furthermore, NdhV was co-located with hydrophilic subunits of NDH-1 loosely associated with the NDH-1L, NDH-1MS' and NDH-1M complexes. The level of the NdhV was significantly increased at high light and deletion of NdhV suppressed the up-regulation of NDH-1 activity, causing the lowered the photosynthetic oxygen evolution at pH 6.5 and high light. These data indicate that NdhV is an intrinsic subunit of hydrophilic subcomplex of NDH-1, required for efficient operation of cyclic electron transport around photosystem I and CO2 uptake at high lights.
学科主题	Multidisciplinary Sciences
出版地	LONDON
WOS关键词	CYCLIC ELECTRON-TRANSPORT ; PYRIDINE-NUCLEOTIDE DEHYDROGENASE ; RESPIRATORY COMPLEX I ; DOMAIN-LIKE FOLD ; NADPH DEHYDROGENASE ; PHOTOSYSTEM-I ; SP PCC-6803 ; CO2 UPTAKE ; THERMOSYNECHOCOCCUS-ELONGATUS ; INTERSYSTEM CHAIN
WOS研究方向	Science Citation Index Expanded (SCI-EXPANDED)
语种	英语
出版者	NATURE PUBLISHING GROUP
WOS记录号	WOS:000378225300002
资助机构	State Key Basic Research and Development Plan 973National Basic Research Program of China [2013CB127005, 2015CB150104] ; National Natural Scientific Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31270286, 31470338] ; Shanghai Science Foundation [13DJ1400102]
内容类型	期刊论文
源URL	[http://ir.ibcas.ac.cn/handle/2S10CLM1/25308]
专题	中科院光生物学重点实验室
作者单位	1.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 2.Chinese Acad Sci, Inst Bot, Key Lab Photobiol, Beijing 100093, Peoples R China 3.Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Plant Physiol & Ecol, Natl Key Lab Plant Mol Genet, 300 Fenglin Rd, Shanghai 200032, Peoples R China
推荐引用方式 GB/T 7714	Chen, Xin,He, Zhihui,Xu, Min,et al. NdhV subunit regulates the activity of type-1 NAD(P)H dehydrogenase under high light conditions in cyanobacterium Synechocystis sp PCC 6803[J]. SCIENTIFIC REPORTS,2016,6.
APA	Chen, Xin,He, Zhihui,Xu, Min,Peng, Lianwei,&Mi, Hualing.(2016).NdhV subunit regulates the activity of type-1 NAD(P)H dehydrogenase under high light conditions in cyanobacterium Synechocystis sp PCC 6803.SCIENTIFIC REPORTS,6.
MLA	Chen, Xin,et al."NdhV subunit regulates the activity of type-1 NAD(P)H dehydrogenase under high light conditions in cyanobacterium Synechocystis sp PCC 6803".SCIENTIFIC REPORTS 6(2016).