9-cis-Neoxanthin in Light Harvesting Complexes of Photosystem II Regulates the Binding of Violaxanthin and Xanthophyll Cycle. Issue 1 (20th March 2017)
- Record Type:
- Journal Article
- Title:
- 9-cis-Neoxanthin in Light Harvesting Complexes of Photosystem II Regulates the Binding of Violaxanthin and Xanthophyll Cycle. Issue 1 (20th March 2017)
- Main Title:
- 9-cis-Neoxanthin in Light Harvesting Complexes of Photosystem II Regulates the Binding of Violaxanthin and Xanthophyll Cycle
- Authors:
- Wang, Ke
Tu, Wenfeng
Liu, Cheng
Rao, Yan
Gao, Zhimin
Yang, Chunhong - Abstract:
- Abstract : The coordination of 9-cis-neoxanthin and violaxanthin in trimeric LHCII directly affect the operation of the xanthophyll cycle and the dynamics of transiently generated NPQ. Abstract: The light-harvesting chlorophyll a/b complex of photosystem II (LHCII) is able to switch to multiple functions under different light conditions (i.e. harvesting solar energy for photosynthesis and dissipating excess excitation energy for photoprotection). The role of the different carotenoids bound to LHCII in regulating the structure and function of the complex is a long-lasting question in photosynthesis research. 9-cis-Neoxanthin (Nx ) is one of the important carotenoids, which can only be found in the LHCIIs. High-resolution structural analysis of LHCII shows that Nx is located between different monomeric LHCIIs, with one side protruding into the lipid membrane. In this study, the various functional significances of this unique feature of Nx binding in LHCII are studied with the in vitro reconstituted LHCIIs both with and without Nx and the native complexes isolated either from wild-type Arabidopsis ( Arabidopsis thaliana ) or from its mutant aba4-3 lacking Nx . Our results reveal that the binding of Nx affects the binding affinity of violaxanthin (Vx ) to LHCII significantly. In the absence of Nx, Vx has a much higher binding affinity to trimeric LHCII. The strong coordination between Nx and Vx at the interfaces of adjacent monomers of LHCII plays an important role both inAbstract : The coordination of 9-cis-neoxanthin and violaxanthin in trimeric LHCII directly affect the operation of the xanthophyll cycle and the dynamics of transiently generated NPQ. Abstract: The light-harvesting chlorophyll a/b complex of photosystem II (LHCII) is able to switch to multiple functions under different light conditions (i.e. harvesting solar energy for photosynthesis and dissipating excess excitation energy for photoprotection). The role of the different carotenoids bound to LHCII in regulating the structure and function of the complex is a long-lasting question in photosynthesis research. 9-cis-Neoxanthin (Nx ) is one of the important carotenoids, which can only be found in the LHCIIs. High-resolution structural analysis of LHCII shows that Nx is located between different monomeric LHCIIs, with one side protruding into the lipid membrane. In this study, the various functional significances of this unique feature of Nx binding in LHCII are studied with the in vitro reconstituted LHCIIs both with and without Nx and the native complexes isolated either from wild-type Arabidopsis ( Arabidopsis thaliana ) or from its mutant aba4-3 lacking Nx . Our results reveal that the binding of Nx affects the binding affinity of violaxanthin (Vx ) to LHCII significantly. In the absence of Nx, Vx has a much higher binding affinity to trimeric LHCII. The strong coordination between Nx and Vx at the interfaces of adjacent monomers of LHCII plays an important role both in operating the xanthophyll cycle and in the transient modulation of nonphotochemical quenching. … (more)
- Is Part Of:
- Plant physiology. Volume 174:Issue 1(2017)
- Journal:
- Plant physiology
- Issue:
- Volume 174:Issue 1(2017)
- Issue Display:
- Volume 174, Issue 1 (2017)
- Year:
- 2017
- Volume:
- 174
- Issue:
- 1
- Issue Sort Value:
- 2017-0174-0001-0000
- Page Start:
- 86
- Page End:
- 96
- Publication Date:
- 2017-03-20
- Subjects:
- Plant physiology -- Periodicals
Botany -- Periodicals
Periodicals
Electronic journals
571.2 - Journal URLs:
- https://academic.oup.com/plphys/issue ↗
http://www.plantphysiol.org/ ↗
http://www.jstor.org/journals/00320889.html ↗
http://www.pubmedcentral.nih.gov/tocrender.fcgi?journal=69 ↗
http://www-us.ebsco.com/online/direct.asp?JournalID=101725 ↗
http://www.oxfordjournals.org/ ↗ - DOI:
- 10.1104/pp.17.00029 ↗
- Languages:
- English
- ISSNs:
- 0032-0889
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 17407.xml