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N-glycosylation and dimerization regulate the PtrMAN6 enzyme activity that may modulate generation of oligosaccharide signals.

Identifieur interne : 002576 ( Main/Exploration ); précédent : 002575; suivant : 002577

N-glycosylation and dimerization regulate the PtrMAN6 enzyme activity that may modulate generation of oligosaccharide signals.

Auteurs : Yunjun Zhao [République populaire de Chine] ; Qian Zhang [République populaire de Chine] ; Luxia Yuan [République populaire de Chine] ; Rui Zhang [République populaire de Chine] ; Laigeng Li [République populaire de Chine]

Source :

RBID : pubmed:24184917

Descripteurs français

English descriptors

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.

DOI: 10.4161/psb.26956
PubMed: 24184917
PubMed Central: PMC4091382


Affiliations:


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Le document en format XML

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<div type="abstract" xml:lang="en">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.</div>
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<Citation>J Exp Bot. 2012 Jun;63(11):3976-88</Citation>
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<ArticleId IdType="pubmed">22553284</ArticleId>
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<li>République populaire de Chine</li>
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<name sortKey="Zhao, Yunjun" sort="Zhao, Yunjun" uniqKey="Zhao Y" first="Yunjun" last="Zhao">Yunjun Zhao</name>
</noRegion>
<name sortKey="Li, Laigeng" sort="Li, Laigeng" uniqKey="Li L" first="Laigeng" last="Li">Laigeng Li</name>
<name sortKey="Yuan, Luxia" sort="Yuan, Luxia" uniqKey="Yuan L" first="Luxia" last="Yuan">Luxia Yuan</name>
<name sortKey="Zhang, Qian" sort="Zhang, Qian" uniqKey="Zhang Q" first="Qian" last="Zhang">Qian Zhang</name>
<name sortKey="Zhang, Rui" sort="Zhang, Rui" uniqKey="Zhang R" first="Rui" last="Zhang">Rui Zhang</name>
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