Functional characterization of persimmon β-galactosidase gene DkGAL1 in tomato reveals cell wall modification related to fruit ripening and radicle elongation

Plant Science ◽  
2018 ◽  
Vol 274 ◽  
pp. 109-120 ◽  
Author(s):  
Qiuyan Ban ◽  
Ye Han ◽  
Yiheng He ◽  
Mijing Jin ◽  
Shoukun Han ◽  
...  
2020 ◽  
Vol 20 (1) ◽  
Author(s):  
Cheng Xue ◽  
Si-Cong Guan ◽  
Jian-Qing Chen ◽  
Chen-Jin Wen ◽  
Jian-Fa Cai ◽  
...  

Abstract Background Pectin methylesterase (PME) is a hydrolytic enzyme that catalyzes the demethylesterification of homogalacturonans and controls pectin reconstruction, being essential in regulation of cell wall modification. During fruit ripening stage, PME-mediated cell wall remodeling is an important process to determine fruit firmness and softening. Strawberry fruit is a soft fruit with a short postharvest life, due to a rapid loss of firm texture. Hence, preharvest improvement of strawberry fruit rigidity is a prerequisite for extension of fruit refreshing time. Although PME has been well characterized in model plants, knowledge regarding the functionality and evolutionary property of PME gene family in strawberry remain limited. Results A total of 54 PME genes (FvPMEs) were identified in woodland strawberry (Fragaria vesca ‘Hawaii 4’). Phylogeny and gene structure analysis divided these FvPME genes into four groups (Group 1–4). Duplicate events analysis suggested that tandem and dispersed duplications effectively contributed to the expansion of the PME family in strawberry. Through transcriptome analysis, we identified FvPME38 and FvPME39 as the most abundant-expressed PMEs at fruit ripening stages, and they were positively regulated by abscisic acid. Genetic manipulation of FvPME38 and FvPME39 by overexpression and RNAi-silencing significantly influences the fruit firmness, pectin content and cell wall structure, indicating a requirement of PME for strawberry fruit softening. Conclusion Our study globally analyzed strawberry pectin methylesterases by the approaches of phylogenetics, evolutionary prediction and genetic analysis. We verified the essential role of FvPME38 and FvPME39 in regulation of strawberry fruit softening process, which provided a guide for improving strawberry fruit firmness by modifying PME level.


2011 ◽  
Vol 5 (S7) ◽  
Author(s):  
Nicky Creux ◽  
Minique De Castro ◽  
Martin Ranik ◽  
Antanas Spokevicius ◽  
Gerd Bossinger ◽  
...  

2019 ◽  
Vol 19 (1) ◽  
Author(s):  
Timo Engelsdorf ◽  
Lars Kjaer ◽  
Nora Gigli-Bisceglia ◽  
Lauri Vaahtera ◽  
Stefan Bauer ◽  
...  

2019 ◽  
Vol 20 (17) ◽  
pp. 4081 ◽  
Author(s):  
Lin Chen ◽  
Xiaohong Liu ◽  
Xiaojia Huang ◽  
Wei Luo ◽  
Yuming Long ◽  
...  

Invertases (INVs) play essential roles in plant growth in response to environmental cues. Previous work showed that plant invertases can be post-translationally regulated by small protein inhibitors (INVINHs). Here, this study characterizes a proteinaceous inhibitor of INVs in maize (Zm-INVINH4). A functional analysis of the recombinant Zm-INVINH4 protein revealed that it inhibited both cell wall and vacuolar invertase activities from maize leaves. A Zm-INVINH4::green fluorescent protein fusion experiment indicated that this protein localized in the apoplast. Transcript analysis showed that Zm-INVINH4 is specifically expressed in maize sink tissues, such as the base part of the leaves and young kernels. Moreover, drought stress perturbation significantly induced Zm-INVINH4 expression, which was accompanied with a decrease of cell wall invertase (CWI) activities and an increase of sucrose accumulation in both base parts of the leaves 2 to 7 days after pollinated kernels. In summary, the results support the hypothesis that INV-related sink growth in response to drought treatment is (partially) caused by a silencing of INV activity via drought-induced induction of Zm-INVINH4 protein.


2019 ◽  
Vol 19 (1) ◽  
Author(s):  
Timo Engelsdorf ◽  
Lars Kjaer ◽  
Nora Gigli-Bisceglia ◽  
Lauri Vaahtera ◽  
Stefan Bauer ◽  
...  

Author(s):  
Jan Xue ◽  
Pallinti Purushotham ◽  
Justin F Acheson ◽  
Ruoya Ho ◽  
Jochen Zimmer ◽  
...  

Abstract In land plants and algae, cellulose is important for strengthening cell walls and preventing breakage due to physical forces. Though our understanding of cellulose production by cellulose synthase enzymes (CESAs) has seen significant advances for several land plant and bacterial species, functional characterization of this fundamental protein is absent in red algae. Here we identify CESA gene candidates in the calcifying red alga Calliarthron tuberculosum (Ct) using sequence similarity-based approaches and elucidate their phylogenetic relationship with other CESAs from diverse taxa. One gene candidate, CtCESA1, was closely related to other putative red algal CESAs. To test if CtCESA1 encoded a true cellulose synthase, CtCESA1 protein was expressed and purified from insect and yeast expression systems. CtCESA1 showed glucan synthase activity in glucose tracer assays. CtCESA1 activity was relatively low when compared to plant and bacterial CESA activity. In an in vitro assay, a predicted N-terminal starch-binding domain from CtCESA1 bound red algal floridean starch extracts, representing a unique domain in red algal CESAs not present in CESAs from other lineages. When the CtCESA1 gene was introduced into Arabidopsis thaliana cesa mutants, the red algal CtCESA1 partially rescued the growth defects of the primary cell wall cesa6 mutant, but not cesa3 or secondary cell wall cesa7 mutants. A fluorescently tagged CtCESA1 localized to the plasma membrane in the Arabidopsis cesa6 mutant background. This study presents functional evidence validating the sequence annotation of red algal cellulose synthases. The relatively low activity of CtCESA1, partial complementation in Arabidopsis, and presence of unique protein domains suggest that there are likely functional differences between the algal and land plant CESAs.


2018 ◽  
Vol 30 (6) ◽  
pp. 1293-1308 ◽  
Author(s):  
Alison W. Roberts ◽  
Jelle Lahnstein ◽  
Yves S.Y. Hsieh ◽  
Xiaohui Xing ◽  
Kuok Yap ◽  
...  

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