2018
DOI: 10.1007/s11120-018-0575-z
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Genetic characterization of a flap1 null mutation in Arabidopsis npq4 and pgr5 plants suggests that the regulatory role of FLAP1 involves the control of proton homeostasis in chloroplasts

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Cited by 10 publications
(15 citation statements)
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“…PxcA interacts with the cyanobacterial FLAP1 homolog, slr0404 (Sato et al, 2007). We reported that Arabidopsis FLAP1 is found in the thylakoid and envelope membrane of chloroplasts and that a flap1 mutant had a greater NPQ value than WT, especially under fluctuating light (Sato et al, 2017;Trinh et al, 2019); the phenotype is similar to those observed in dldg1 (Fig. 4B).…”
Section: Discussionsupporting
confidence: 60%
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“…PxcA interacts with the cyanobacterial FLAP1 homolog, slr0404 (Sato et al, 2007). We reported that Arabidopsis FLAP1 is found in the thylakoid and envelope membrane of chloroplasts and that a flap1 mutant had a greater NPQ value than WT, especially under fluctuating light (Sato et al, 2017;Trinh et al, 2019); the phenotype is similar to those observed in dldg1 (Fig. 4B).…”
Section: Discussionsupporting
confidence: 60%
“…We screened for Arabidopsis genes that have the following properties: (i) predicted to be chloroplastic, (ii) co-expressed with known NPQ-related genes, and (iii) conserved in oxygenic phototrophs. In addition to FLAP1, the details of which we reported previously (Sato et al, 2017;Trinh et al, 2019), we identified, by reverse genetic screening, another candidate NPQ-related gene at the open-reading frame, At4g31040, which we abbreviated as DLDG1. Examination of the co-expression database ATTEDII (Obayashi et al, 2018) revealed that DLDG1 is co-expressed with NPQ1 (encodes VDE), FTRA2 (ferredoxin-thioredoxin oxidoreductase subunit A), and FNR2 (ferredoxin-NADP + oxidoreductase 2), whose functions seem to be important for controlling NPQ and ΔpH.…”
Section: Identification Of a Candidate Gene Responsible For Controllimentioning
confidence: 98%
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“…At the same time, plants grown under monochromatic green light or mixed red–green–blue spectrum had significantly diminished levels of PsbS, cyt f , and PGRL1 protein. The importance of the PsbS and PGR5/PGRL1 complex in NPQ activation was previously documented with npq4 and pgr5 (also pgr1 ) mutants, which are defective in PsbS-dependent NPQ and proton influx from the stroma to the lumen [ 48 ], respectively. Several authors [ 7 , 26 , 47 , 48 , 49 ] have documented that accelerated NPQ formation induced by pre-illumination was absent in npq4 , which presented almost no NPQ formation, while in the pgr1 mutant, the NPQ rise was visibly slowed down and sensitive to DTT feeding [ 26 ].…”
Section: Discussionmentioning
confidence: 99%
“…The extreme sensitivity of pgr5 loss-of-function mutants to fluctuating light has been reported many times by independent groups [25, 26, 29]. The susceptibility is primarily attributed to a malfunctioning cyclic electron flow (CEF) cycle around PSI [20].…”
Section: Resultsmentioning
confidence: 99%