2015
DOI: 10.1016/j.jphotobiol.2015.11.002
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Excitation energy transfer and charge separation are affected in Arabidopsis thaliana mutants lacking light-harvesting chlorophyll a/b binding protein Lhcb3

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Cited by 19 publications
(16 citation statements)
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“…The eighteen rice genes reported here have homologs in Arabidopsis for which tagged mutants are available ( Table 2 ). Nine of them ( CPFTSY , NDH-O , SOQ1 , LHCB3 , RRF , PGRL1B , HCF244 , NAD(P)-linked oxidoreductase, and MRL1 ) were annotated to be involved in the photosynthesis process [ 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 ]. Moreover, the homolog of LOC_Os11g43600 is CPRF1, an Arabidopsis gene required for chloroplast development [ 33 ].…”
Section: Resultsmentioning
confidence: 99%
“…The eighteen rice genes reported here have homologs in Arabidopsis for which tagged mutants are available ( Table 2 ). Nine of them ( CPFTSY , NDH-O , SOQ1 , LHCB3 , RRF , PGRL1B , HCF244 , NAD(P)-linked oxidoreductase, and MRL1 ) were annotated to be involved in the photosynthesis process [ 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 ]. Moreover, the homolog of LOC_Os11g43600 is CPRF1, an Arabidopsis gene required for chloroplast development [ 33 ].…”
Section: Resultsmentioning
confidence: 99%
“…The current study revealed that rice GDCH (A3C6G9) was acetylated at the 156th lysine site, while LFNR1 (Q0DF89) harbored acetylation modifications on 79th and 188th lysine, and their acetylation intensities in leaf were significantly higher than those in other tissues. In addition, Chlorophyll A-B binding proteins (Q5ZA98, Q6Z411 and Q53N82), which are responsible for the capturing and delivering of excitation energy to photosystems [ 46 ], as well as sucrose synthases participating in starch metabolism (P31924, P30298 and Q43009), also showed similar acetylated patterns in leaf, suggesting the extensive regulatory roles of PKA on photosynthesis in leaf.…”
Section: Discussionmentioning
confidence: 99%
“…Indeed the binding of this trimer is affected in kolhcb6 mutant plants and Lhcb3 is depleted, showing a strong link between the two proteins [68]. On the contrary, in Lhcb3 mutant plants, CP24 is not depleted; in this case the only changes are an increase in Lhcb1 and Lhcb2 isoforms, which likely replace Lhcb3 in the M trimers, and the different orientation and strength of binding of the M-LHCII trimer to PSII [17,67,69]. Lack of Lhcb3 induces indeed a rotation of about 21° of the M trimer compared to its position in WT plants [67].…”
Section: Lhcb3 a Special Lhcii Isoform Of Plant Psiimentioning
confidence: 95%
“…If Damkjaer and co-workers found no depletion of PSII activity in koLhcb3 plants [67], Adamiec and coworkers, by using a biochemical and time resolved fluorescence approach, found that PSII antenna size was slightly increased and excitation energy transfer slightly decreased in the koLhcb3 mutant. This is likely due to a less efficient transfer between the Lhcb3-depleted M trimer and the neighboring CP24 and CP29 [69], which could be explained by the positional shift of the M trimer. Additional studies of the energy transfer in both WT and Lhcb3-depleted plants, as well as in plants that have lost Lhcb3 and/or CP24, such as the Pinus and Picea lines [33], are necessary to fully understand the role of Lhcb3.…”
Section: Lhcb3 a Special Lhcii Isoform Of Plant Psiimentioning
confidence: 99%