Chlorophyll biosynthesis and chloroplast development in etiolated seedlings of Ginkgo biloba L.

2009 ◽  
Vol 47 (4) ◽  
pp. 510-516 ◽  
Author(s):  
A. Pavlovic ◽  
L. Slovakova ◽  
V. Demko ◽  
M. Durchan ◽  
K. Mikulova ◽  
...  
Keyword(s):  
Ginkgo Biloba ◽  
Chloroplast Development ◽  
Chlorophyll Biosynthesis ◽  
Etiolated Seedlings

scholarly journals Construction and analysis of a library of miRNA in gold-coloured mutant leaves of Ginkgo biloba L.

2019 ◽  
Vol 31 (1) ◽  
pp. 81-92 ◽  
Author(s):  
Weixing Li ◽  
Zhichong He ◽  
Shunbo Yang ◽  
Yunling Ye ◽  
Huiru Jiang ◽  
...  
Keyword(s):  
Expression Pattern ◽  
Transcriptome Analysis ◽  
Ginkgo Biloba ◽  
Regulatory Networks ◽  
Target Genes ◽  
Chloroplast Development ◽  
Glutathione Metabolism ◽  
Hormone Metabolism ◽  
Srna Library ◽  
Normal Green

AbstractTo gain insights into the regulatory networks of miRNAs related to golden colour formation in Ginkgo biloba leaves, we constructed an sRNA library of golden-green striped mutant leaves. A total of 213 known miRNAs comprising 54 miRNA families were obtained, and 214 novel miRNAs were identified in the mutant leaves. We further constructed a normal green leaf sRNA library as a control and compared the expression of miRNAs between mutant and normal leaves. We found 42 known and 54 novel differential expression candidate miRNAs; 39 were up-regulated and 57 down-regulated in mutants compared to normal leaves. Our transcriptome analysis and annotation of the predicted targets indicated that the potential roles of miRNAs in G. biloba leaves included involvement in the ‘Glutathione metabolism’, ‘Plant circadian rhythm’, and ‘Phenylalanine metabolism’ categories. miRNAs and their targets were further validated by qRT-PCR. The expression of miR159a and miR159c, in particular, was significantly higher in mutant leaves than in normal leaves, while their potential target gene CLT3, which is associated with chloroplast development, displayed the opposite expression pattern. In addition, the expression of miR396g-3p and miR396h was also significantly higher in mutant leaves than in normal leaves, while the target genes ABP1 (auxin-related gene) and PPR32 (chloroplast RNA editing protein), respectively, showed the opposite expression pattern. Combined with the transcriptome analysis, these data suggest that miR159, miR396, and their targets may participate in chloroplast development and hormone metabolism to regulate colour formation in G. biloba leaves.

scholarly journals Rice TSV2 Encoding Threonyl-tRNA Synthetase is Needed for Early Chloroplast Development and Seedling Growth under Cold Stress

2021 ◽  
Author(s):  
Dongzhi Lin ◽  
Wenhao Zhou ◽  
Yulu Wang ◽  
Jia Sun ◽  
Xiaobiao Pan ◽  
...  
Keyword(s):  
Cold Stress ◽  
Chloroplast Development ◽  
Chlorophyll Biosynthesis ◽  
Trna Synthetase ◽  
Loss Of Function ◽  
Specific Expression ◽  
Trna Synthetases ◽  
Leaf Stage ◽  
Virescent Mutant ◽  
Albino Phenotype

Abstract Threonyl-tRNA synthetase (ThrRS), one of aminoacyl-tRNA synthetases (AARSs), plays a crucial role in protein synthesis. However, the AARS functions on rice chloroplast development and growth were not fully appraised. In this study, a thermo-sensitive virescent mutant tsv2, which showed albino phenotype and lethal after the 4-leaf stage at 20 °C but recovered to normal when the temperatures rose, was identified and characterized. Map-based cloning and complementation tests showed that TSV2 encoded a chloroplast-located ThrRS protein in rice. The Lys-to-Arg mutation in the anticodon-binding domain hampered chloroplast development under cold stress, while the loss-of-function of the ThrRS core domain in TSV2 fatally led to seedling death regardless of growing temperatures. In addition, TSV2 had a specific expression in early leaves. Its disruption obviously resulted in down-regulation of certain genes associated with chlorophyll biosynthesis, photosynthesis and chloroplast development at cold conditions. Our observations revealed that rice nuclear-encoded TSV2 plays an important role in chloroplast development at the early leaf stage under cold stress.

scholarly journals Characterization and Fine Mapping of a Yellow-Virescent Gene Regulating Chlorophyll Biosynthesis and Early Stage Chloroplast Development in Brassica napus

2020 ◽  
Vol 10 (9) ◽  
pp. 3201-3211 ◽  
Author(s):  
Chuanji Zhao ◽  
Lijiang Liu ◽  
Luqman Bin Safdar ◽  
Meili Xie ◽  
Xiaohui Cheng ◽  
...  
Keyword(s):  
Brassica Napus ◽  
Chloroplast Development ◽  
Early Stage ◽  
Bulked Segregant Analysis ◽  
Chlorophyll Biosynthesis ◽  
Protoporphyrin Ix ◽  
Chloroplast Ultrastructure ◽  
Crop Species ◽  
Chlorophyll Accumulation ◽  
Nucleotide Mutation

Abstract Chlorophyll biosynthesis and chloroplast development are crucial to photosynthesis and plant growth, but their regulatory mechanism remains elusive in many crop species. We isolated a Brassica napus yellow-virescent leaf (yvl) mutant, which exhibited yellow-younger-leaf and virescent-older-leaf with decreased chlorophyll accumulation and delayed chloroplast development. We mapped yvl locus to a 70-kb interval between molecular markers yvl-O10 and InDel-O6 on chromosome A03 in BC2F2 population using whole genome re-sequencing and bulked segregant analysis. The mutant had a ‘C’ to ‘T’ substitution in the coding sequence of BnaA03.CHLH, which encodes putative H subunit of Mg-protoporphyrin IX chelatase (CHLH). The mutation resulted in an imperfect protein structure and reduced activity of CHLH. It also hampered the plastid encoded RNA polymerase which transcribes regulatory genes of photosystem II and I. Consequently, the chlorophyll a/b and carotenoid contents were reduced and the chloroplast ultrastructure was degraded in yvl mutant. These results explain that a single nucleotide mutation in BnaA03.CHLH impairs PEP activity to disrupt chloroplast development and chlorophyll biosynthesis in B. napus.

A rice White-stripe leaf3 (wsl3) mutant lacking an HD domain-containing protein affects chlorophyll biosynthesis and chloroplast development

2016 ◽  
Vol 59 (3) ◽  
pp. 282-292 ◽  
Author(s):  
Shaolu Zhao ◽  
Wuhua Long ◽  
Yihua Wang ◽  
Linglong Liu ◽  
Yunlong Wang ◽  
...  
Keyword(s):  
Chloroplast Development ◽  
Chlorophyll Biosynthesis ◽  
White Stripe

Rice TSV2 Encoding Threonyl-tRNA Synthetase is Needed for Early Chloroplast Development and Seedling Growth under Cold Stress

2020 ◽  
Author(s):  
Dongzhi Lin ◽  
Wenhao Zhou ◽  
Jia Sun ◽  
Yulu Wang ◽  
Xiaobiao Pan ◽  
...  
Keyword(s):  
Plant Growth ◽  
Cold Stress ◽  
Chloroplast Development ◽  
Chlorophyll Biosynthesis ◽  
Trna Synthetase ◽  
Loss Of Function ◽  
Specific Expression ◽  
Trna Synthetases ◽  
Virescent Mutant ◽  
Albino Phenotype

Abstract Background The chloroplast is a vital photosynthetic organelle for plant growth and development. However, the genetic factors involved in chloroplast development and its relationship with environment factors are largely unknown. Threonyl-tRNA synthetase (ThrRS), one of aminoacyl-tRNA synthetases (AARSs), plays a crucial role in protein synthesis. To date, there are few studies for AARS function on chloroplast development and plant growth, much less ThrRS in rice. Result In this paper, we characterized a thermo-sensitive virescent mutant tsv2, which showed albino phenotype and could not survive after the 4-leaf stage when grown at 20 °C, but recovered the normal phenotype when the temperature rose. Map-based cloning and complementation tests showed that TSV2 encoded a chloroplast-located ThrRS protein in rice and the Lys-to-Arg mutation in the anticodon-binding domain affected chloroplast development under cold stress. Furthermore, the loss-of-function of the core domain in TSV2 led to seedling death regardless of temperatures. In addition, TSV2 had a tissue-specific expression, and its disruption resulted in an evidently down-regulation of certain genes associated with chlorophyll biosynthesis, photosynthesis and chloroplast development at cold stress. Conclusion The TSV2 encodes a rice threonyl-tRNA synthetase, located in chloroplasts, which is essential for cold-responsive regulation for chloroplast development and plant growth and closely related to the assembly of chloroplast ribosomes and functions at the first step of chloroplast differentiation.

scholarly journals Differences in Photosynthesis of Variegated Temple Bamboo Leaves with Various Levels of Variegation are Related to Chlorophyll Biosynthesis and Chloroplast Development

2018 ◽  
Vol 143 (2) ◽  
pp. 144-153 ◽  
Author(s):  
Lingyan Chen ◽  
Jinli Lai ◽  
Tianyou He ◽  
Jundong Rong ◽  
Muhammad Waqqas Khan Tarin ◽  
...  
Keyword(s):  
Thylakoid Membrane ◽  
Chloroplast Development ◽  
Chlorophyll Biosynthesis ◽  
Protoporphyrin Ix ◽  
Light Response ◽  
Photosynthetic Parameters ◽  
Leaf Color ◽  
Light Response Curve ◽  
Bamboo Leaves ◽  
Series Of Experiments

Variegated temple bamboo (Sinobambusa tootsik f. luteoloalbostriata) is a species of ornamental bamboo (Bambusoideae) that has gained popularity because of its striped or variegated leaves. In this study, a series of experiments was conducted to determine the factors contributing to the leaf color of this species, which included the content of the photosynthetic pigments and the chlorophyll biosynthetic precursors, the photosynthetic parameters, and the microstructure and ultrastructure of the different phenotypes. Discoloration in the leaves of variegated temple bamboo plants is attributed to two possible pathways. One was a block in chlorophyll biosynthesis, which led to the failure in biosynthesis of the thylakoid membrane. The other one was a disruption in chloroplast development. The lack of thylakoid membrane may have inhibited the conversion of coproporphyrinogen III (Coprogen III) to protoporphyrin IX (Proto IX) during the chlorophyll biosynthesis because the enzyme responsible for this conversion, protogen oxidase, is bound to the thylakoid membrane. The abnormalities in chloroplasts and a low concentration of chlorophyll in the variegated leaves led to a significantly lower photosynthetic rate than in the entirely green leaves, as demonstrated in the light-response curve.

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