ArticlePlant signaling & behavior2013
N-glycosylation and dimerization regulate the PtrMAN6 enzyme activity that may modulate generation of oligosaccharide signals.
Article in Plant signaling & behavior, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
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- Combining single-cell RNA sequencing with spatial transcriptome analysis reveals dynamic molecular maps of cambium differentiation in the primary and secondary growth of trees.Plant communications · 2023Article
- Hidden Relationships betweenInternational journal of molecular sciences · 2022Review
- Engineering Non-cellulosic Polysaccharides of Wood for the Biorefinery.Frontiers in plant science · 2018Article
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PtrMAN6 is a plant mannan endo-hydrolase involved in modulating cell expansion and cell wall thickening in Populus developing xylem. N-glycosylation and dimerization affect the PtrMAN6 enzymatic activity, which is crucial for production of the endogenous galactoglucomannan oligosaccharide signal molecule in plants. There are 5 potential N-glycosylation sites and 6 cysteines in PtrMAN6 sequence. Each of the N-glycosylation or cysteine sites was site-direct mutagenized individually as well as in combination to analyze their effects on the PtrMAN6 N-glycosylation or dimerization status and the enzyme activity. Our results demonstrated that all 5 potential N-glycosylation sites are involved in the N-glycosylation, which is essential for PtrMAN6 enzyme activity. Meanwhile, we found only 3 carboxyl-terminal cysteines are involved in formation of disulfide-linked dimer to regulate PtrMAN6 activity. The 3 carboxyl-terminal cysteines were conserved in the wall-bounded mannan endo-hydrolases, and this structure may play a role in regulating the PtrMAN6 activity through interaction with redox signals such as reactive oxygen species (ROS) and hydrogen sulfide (H2S) for GGMOs signal generation.
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Registered trials
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