Photosystem II supercomplexes lacking light-harvesting antenna protein LHCB5 and their organization in the thylakoid membrane
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F25%3A00618704" target="_blank" >RIV/61389030:_____/25:00618704 - isvavai.cz</a>
Alternative codes found
RIV/61989592:15310/25:73630841 RIV/00216224:14740/25:00143807
Result on the web
<a href="https://doi.org/10.1111/ppl.70167" target="_blank" >https://doi.org/10.1111/ppl.70167</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1111/ppl.70167" target="_blank" >10.1111/ppl.70167</a>
Alternative languages
Result language
angličtina
Original language name
Photosystem II supercomplexes lacking light-harvesting antenna protein LHCB5 and their organization in the thylakoid membrane
Original language description
Light-harvesting protein LHCB5 is one of the three minor antenna proteins (LHCB4-6) that connect the core (C) of photosystem II (PSII) with strongly (S) and moderately (M) bound peripheral trimeric antennae (LHCIIs), forming a dimeric PSII supercomplex known as C2S2M2. Plants lacking LHCB4 and LHCB6 do not form C2S2M2, indicating that these minor antenna proteins are crucial for C(2)S(2)M(2 )assembly. However, studies on antisense asLhcb5 plants suggest this may not apply to LHCB5. Using mild clear-native PAGE (CN-PAGE) and electron microscopy (EM), we separated and structurally characterized the C(2)S(2)M(2 )supercomplex from the Arabidopsis lhcb5 mutant. When compared with wild type (WT), the C(2)S(2)M(2 )supercomplexes in the lhcb5 mutant have slightly different positions of S and M trimers and are generally smaller and present in the thylakoid membrane at higher density. Using CN-PAGE, we did not observe any PSII megacomplexes in the lhcb5 mutant, although they are routinely detected by this method in WT. However, we identified the megacomplexes directly in thylakoid membranes via EM, indicating that the megacomplexes are formed but are too labile to be separated. While in WT, both parallel- and non-parallel-associated PSII supercomplexes can be detected in the thylakoid membrane (Nosek et al., 2017, Plant Journal 89, pp. 104-111), only the parallel-associated PSII supercomplexes were found in the lhcb5 mutant. This finding suggests that the formation of non-parallel-associated PSII supercomplexes depends on the presence of LHCB5. The presence of large PSII supercomplexes and megacomplexes, even though less stable, could explain the WT-like photosynthetic characteristics of the lhcb5 mutant.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
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
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Physiologia Plantarum
ISSN
0031-9317
e-ISSN
1399-3054
Volume of the periodical
177
Issue of the periodical within the volume
2
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
e70167
UT code for WoS article
001450497400001
EID of the result in the Scopus database
2-s2.0-105000940751