Mechanism of photoprotection in the cyanobacterial ancestor of plant antenna proteins
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F15%3A00447354" target="_blank" >RIV/60077344:_____/15:00447354 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/15:00447354 RIV/60076658:12310/15:43888683
Result on the web
<a href="http://dx.doi.org/10.1038/nchembio.1755" target="_blank" >http://dx.doi.org/10.1038/nchembio.1755</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/nchembio.1755" target="_blank" >10.1038/nchembio.1755</a>
Alternative languages
Result language
angličtina
Original language name
Mechanism of photoprotection in the cyanobacterial ancestor of plant antenna proteins
Original language description
Plants collect light for photosynthesis using light-harvesting complexes (LHCs)-an array of chlorophyll proteins that are able to reversibly switch from harvesting to energy-dissipation mode to prevent damage of the photosynthetic apparatus. LHC antennae as well as other members of the LHC superfamily evolved from cyanobacterial ancestors called high light-inducible proteins (Hlips). Here, we characterized a purified Hlip family member HliD isolated from the cyanobacterium Synechocystis sp. PCC 6803. We found that the HliD binds chlorophyll-a (Chl-a) and beta-carotene and exhibits an energy-dissipative conformation. Using femtosecond spectroscopy, we demonstrated that the energy dissipation is achieved via direct energy transfer from a Chl-a Q(y) state to the beta-carotene S-1 state. We did not detect any cation of beta-carotene that would accompany Chl-a quenching. These results provide proof of principle that this quenching mechanism operates in the LHC superfamily and also shed light on the photoprotective role of Hlips and the evolution of LHC antennae.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
BO - Biophysics
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Nature Chemical Biology
ISSN
1552-4450
e-ISSN
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Volume of the periodical
11
Issue of the periodical within the volume
4
Country of publishing house
US - UNITED STATES
Number of pages
5
Pages from-to
287-291
UT code for WoS article
000351666500012
EID of the result in the Scopus database
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