scholarly journals Implications of the galactosidase activity of yieldin in the regulatory mechanism of yield threshold that is fundamental to cell wall extension

2018 ◽  
Vol 163 (2) ◽  
pp. 259-266 ◽  
Author(s):  
Akane Okamoto-Nakazato
1995 ◽  
pp. 91-98 ◽  
Author(s):  
H. Nonami ◽  
K. Tanimoto ◽  
A. Tabuchi ◽  
T. Fukuyama ◽  
Y. Hashimoto

2020 ◽  
Author(s):  
Pieter Nibbering ◽  
Bent L. Petersen ◽  
Mohammed Saddik Motawia ◽  
Bodil Jørgensen ◽  
Peter Ulvskov ◽  
...  

AbstractPlant arabinogalactan proteins (AGPs) are a diverse group of cell surface- and wall-associated glycoproteins. Functionally important AGP glycans are synthesized in the Golgi apparatus, but the relationships between their glycosylation, processing, and functionality are poorly understood. Here we report the identification and functional characterization of two Golgi-localized exo-β-1,3-galactosidases from the glycosyl hydrolase 43 (GH43) family in Arabidopsis thaliana. GH43 loss of function mutants exhibit root cell expansion defects in sugar-containing growth media. This root phenotype is associated with an increase in the extent of AGP cell wall association, as demonstrated by Yariv phenylglycoside dye quantification and comprehensive microarray polymer profiling of sequentially extracted cell walls. Recombinant GH43 characterization showed that the exo-β-1,3-galactosidase activity of GH43s is hindered by β-1,6 branches on β-1,3-galactans. In line with this steric hindrance, the recombinant GH43s did not release galactose from cell wall extracted glycoproteins or AGP rich gum arabic. These results show that Arabidopsis GH43s are involved in AGP glycan biosynthesis in the Golgi, and suggest their exo-β-1,3-galactosidase activity influences AGP and cell wall matrix interactions, thereby adjusting cell wall extensibility.


Nature ◽  
1971 ◽  
Vol 229 (5285) ◽  
pp. 458-458

2019 ◽  
Vol 85 (21) ◽  
Author(s):  
Liqin Kang ◽  
Jiangsheng Zhou ◽  
Rui Wang ◽  
Xingwei Zhang ◽  
Cuicui Liu ◽  
...  

ABSTRACT This study reports that a high concentration of the endo-β-1,3-glucanase ENG (200 μg ml−1) induced heat-inactivated stipe wall extension of Coprinopsis cinerea, whereas a high concentration of the extracellular β-glucosidase BGL2 (1,000 μg ml−1) did not; however, in combination, low concentrations of ENG (25 μg ml−1) and BGL2 (260 μg ml−1) induced heat-inactivated stipe cell wall extension. In contrast to the previously reported chitinase-reconstituted stipe wall extension, β-1,3-glucanase-reconstituted heat-inactivated stipe cell wall extension initially exhibited a fast extension rate that quickly decreased to zero after approximately 60 min; the stipe cell wall extension induced by a high concentration of β-1,3-glucanase did not result in stipe breakage during measurement, and the inner surfaces of glucanase-reconstituted extended cell walls still remained as amorphous matrices that did not appear to have been damaged. These distinctive features of the β-1,3-glucanase-reconstituted wall extension may be because chitin chains are cross-linked not only to the nonreducing termini of the side chains and the backbones of β-1,6 branched β-1,3-glucans but also to other polysaccharides. Remarkably, a low concentration of either the β-1,3-glucanase ENG or of chitinase ChiE1 did not induce heat-inactivated stipe wall extension, but a combination of these two enzymes, each at a low concentration, showed stipe cell wall extension activity that exhibited a steady and continuous wall extension profile. Therefore, we concluded that the stipe cell wall extension is the result of the synergistic actions of glucanases and chitinases. IMPORTANCE We previously reported that the chitinase could induce stipe wall extension and was involved in stipe elongation growth of the mushroom Coprinopsis cinerea. In this study, we explored that β-1,3-glucanase also induced stipe cell wall extension. Interestingly, the extension profile and extended ultra-architecture of β-1,3-glucanase-reconstituted stipe wall were different from those of chitinase-reconstituted stipe wall. However, β-1,3-glucanase cooperated with chitinase to induce stipe cell wall extension. The significance of this synergy between glucanases and chitinases is that it enables a low concentration of active enzymes to induce wall extension, and the involvement of β-1,3-glucanases is necessary for the cell wall remodeling and the addition of new β-glucans during stipe elongation growth.


1992 ◽  
Vol 4 (11) ◽  
pp. 1425-1433 ◽  
Author(s):  
S McQueen-Mason ◽  
D M Durachko ◽  
D J Cosgrove

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