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Side chain modifications of phyllobilins are not essential for chlorophyll degradation during dark-induced senescence in Arabidopsis

ABSTRACT: Side chain modifications of phyllobilins are not essential for chlorophyll degradation during dark-induced senescence in Arabidopsis

PROVIDER: PRJEB52187 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	ERR9551710.fastq.gz	Fastqsanger.gz
	ERR9551720.fastq.gz	Fastqsanger.gz
	ERR9551730.fastq.gz	Fastqsanger.gz
	ERR9551711.fastq.gz	Fastqsanger.gz
	ERR9551721.fastq.gz	Fastqsanger.gz

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Similar Datasets

Side chain modifications of phyllobilins are not essential for chlorophyll degradation during dark-induced senescence in Arabidopsis

Project description:Detached leaf of mutants from Arabidopsis thaliana mutants from WTcol, TIC55, CYP89a9, MES16 and triple mutant CYP89a9 TIC55 and MES16 incubated in the dark for 3 days.

2022-07-01 | E-MTAB-11614 | biostudies-arrayexpress

Chlorophyll degradation

Project description:Chlorophyll degradation by aerobic marine bacterium

| PRJEB15523 | ENA

Transcriptome profiling of Arabidopsis mutants of the chlorophyll degradation PAO/Phyllobilin pathway

Project description:Detoxification of chlorophyll during leaf senescence in higher plants is a complex and tightly regulated process. It aims at opening the chlorophyll porphyrin ring to produce non-photoreactive degradation products, termed phyllobilins, which are stored in the vacuole. Here we are describing the influence on the transcriptome of dark-induced senescing leaf of the removal of three key enzymes of the PAO/phyllobilin pathway (namely: PAO, PPH and NYE/SGR).

2018-12-31 | E-MTAB-6965 | biostudies-arrayexpress

Side-chain modifications of phyllobilins may not be essential for chlorophyll degradation in <i>Arabidopsis</i>.

Project description:Disposing efficiently and safely chlorophyll derivatives during senescence requires a coordinated pathway that is well conserved throughout green plants. The PAO/phyllobilin pathway catalyzes the degradation of the chlorophyll during senescence and allows detoxification of the pigment and its subsequent export from the chloroplast. Although most of the chloroplastic reactions involved in chlorophyll degradation are well understood, the diversity of enzymes responsible for downstream modifications of non-phototoxic phyllobilins remains to be explored. More than 40 phyllobilins have been described to date, but only three enzymes catalyzing side-chain reactions have been identified in Arabidopsis thaliana, namely, TIC55, CYP89A9, and MES16. Here, by generating a triple mutant, we evaluate the extent to which these enzymes are influencing the rate and amplitude of chlorophyll degradation at the metabolite as well as its regulation at the transcriptome level. Our data show that major side-chain modifications of phyllobilins do not influence significantly chlorophyll degradation or leaf senescence, letting the physiological relevance of their striking diversity an open question.

| S-EPMC9399834 | biostudies-literature

Comparative analysis of D. shibae wild-type vs. ∆luxI1 supplemented with acetylated homoserine-lactones with different length of the side chain and modifications

2014-04-01 | GSE54420 | GEO

Comparative analysis of D. shibae wild-type vs. M-bM-^HM-^FluxI1 supplemented with acetylated homoserine-lactones with different length of the side chain and modifications

Project description:Comparison of a quorum sensing null mutant supplemented with AHLs with different length of the side chain and modifications with D. shibae wild-type in order to identify traits induced by distinct autoinducers in this organism. Loop-design, two to three biological replicates of D. shibae wild-type, M-bM-^HM-^FluxI1 and M-bM-^HM-^FluxI1 supplemented with 500 nM C18-HSL, C18en-HSL and C18dien-HSL at cultivation start. Samples were taken in mid-exponential growth phase at OD600 0.4

2014-04-01 | E-GEOD-54420 | biostudies-arrayexpress

Expression data from dark grown Arabidopsis Wild type (Wt, col-o) and pif1-2 (At2g20810, Salk_072677) mutant seedlings

Project description:Arabidopsis bHLH transcription factor PIF1 has been shown function as a negative regulator of Chlorophyll biosynthesis. Pif1-2 mutant accumulate more protochlorophylide during prolonged dark growth condations, therefore the comparation between Wt and pif1-2 mutant will help us find the PIF1 target genes in Chlorophyll biosynthesis pathway at genome wide level under the dark grown conditions. We used microarrays to detail the global gene expression under the regulation of PIF1. Keywords: Genotype comparison

2008-05-30 | GSE11594 | GEO

ANAC046, a NAC family transcription factor, is involved in leaf senescence by controlling the chlorophyll catabolic gene expression in Arabidopsis

Project description:Chlorophyll (Chl) degradation is an important process during leaf senescence, bud breaking and fruit ripening. Chlorophyll catabolic pathway has been intensively studied and nearly all the enzymes involved in the pathway are characterized. However, regulatory mechanism of the pathway is largely unknown at the molecular level. In this study, we performed a yeast one-hybrid screening using a library composed only of transcription factor cDNAs to search for factors controlling expression of the chlorophyll catabolic genes. We identified a common regulator, ANAC046, that directly binds to the promoter regions of NON-YELLOW COLORING 1, STAY-GREEN 1 (SGR1), SGR2, and pheophorbide a oxygenase. Transgenic plants overexpressing ANAC046 exhibited an early senescence phenotype with lower chlorophyll content as compared with the wild-type plants, while loss-of-function mutants exhibited a delayed senescence phenotype with higher chlorophyll content. Microarray analysis of ANAC046 showed that not only chlorophyll catabolic genes but also senescence-associated genes were positively regulated by ANAC046. Here, we demonstrate that ANAC046 is a novel positive regulator of Arabidopsis leaf senescence and exerts its effect through controlling the expressions of Chl catabolic genes and senescence-associated genes. Transcriptomes of leaf of ANAC046-overexpression plant (50 days after seed sawing), seedling of ANAC046-SRDX-overexpression plant (5 days after dark treatment), and seedling of ANAC046-knockout plant (5 days after dark treatment) were measured together with their respective wild-type controls.

2016-04-01 | E-GEOD-71767 | biostudies-arrayexpress

Overexpression of 7-hydroxymethyl Chlorophyll a Reductase from Cucumber in Tobacco Accelerates Dark-Induced Chlorophyll Degradation.

Project description:7-hydroxymethyl chlorophyll (Chl) a reductase (HCAR) plays critical roles in the Chl cycle and degradation during leaf senescence, however, its function in horticultural crops remains unknown. Here, we identified an HCAR gene (CsHCAR) from cucumber (Cucumis sativus L.) and investigated its roles in response to dark-induced Chl degradation. CsHCAR encoded 459 amino acids, which were orthologous to Arabidopsis HCAR, had the conserved domains, and localized in the chloroplast. Gene expression analysis showed that CsHCAR expression was the highest in senescent leaves and was responsive to different stresses and phytohormone treatments. Overexpression of CsHCAR in tobacco accelerated dark-induced Chl degradation through enhancing the expression of Chl catabolic genes. After 10 d of darkness treatment, the biomass of CsHCAR overexpression plants was reduced. Furthermore, the value of net photosynthetic rate, maximum quantum yield of photosystem II, and effective quantum yield of photosystem II in CsHCAR overexpression plants was significantly reduced in comparison to that in wild-type (WT) plants. The photosynthetic protein content, including Lhcb1, Lhcb2, Lhcb4, RbcS, and RbcL in CsHCAR overexpression plants exhibited a lower level as compared to that observed in WT plants. In addition, the expression of genes encoding these proteins in CsHCAR overexpression plants was significantly lower than that in WT plants. Moreover, CsHCAR overexpression plants inhibited the dark-induced accumulation of reactive oxygen species (ROS). These results indicate that CsHCAR affects the stability of photosynthetic proteins in chloroplasts, positively regulates Chl degradation, and plays an important role in maintaining ROS homeostasis in leaves.

| S-EPMC8465020 | biostudies-literature

Mutation in a chlorophyll binding motif of Brassica ferrochelatase enhances both heme and chlorophyll biosynthesis

Project description:The heme branch of tetrapyrrole biosynthesis contributes to the regulation of chlorophyll levels. However, the molecular mechanism underlying the balance between chlorophyll and heme synthesis remains elusive. Here, we identified a dark green leaf mutant dg, which contains high levels of chlorophyll b, from an ethyl methanesulfonate (EMS) -induced mutant library of Chinese cabbage. The dg phenotype is attributed to a nonsynonymous homozygous mutation in ferrochelatase 2 (BrFC2), leading to an arginine (R) to lysine (K) amino acid substitution in the conserved chlorophyll a/b-binding motif (CAB) of BrFC2. Overexpression of mutated BrFC2 (dBrFC2) in Chinese cabbage results in a pronounced phenotype associated with the dark green leaves, in contrast to transgenic lines overexpressing wild-type BrFC2 with a low-chlorophyll phenotype. Increased dBrFC2 homodimer formation stimulates heme production in dg compared with wildtype BrFC2. Moreover, we found that dBrFC2 interacts with protochlorophyllide oxidoreductase B1 and B2 (BrPORB1 and BrPORB2) to enhance their binding ability to substrate protochlorophyllide (Pchlide), thereby promoting BrPORBs-catalyzed production of chlorophyllide (Chlide) that can be directly converted into chlorophyll. Our results reveal that dBrFC2 is a strong gain-of-function mutation contributing to balancing heme and chlorophyll synthesis via a novel regulatory mechanism in which dBrFC2 promotes BrPORB enzymatic reaction to enhance chlorophyll synthesis.

2022-10-09 | PXD037223 |

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