Yariv reactivity of type II arabinogalactan from larch wood

Sato, Kazuki; Hara, Katsuya; Yoshimi, Yoshihisa; Kitazawa, Kiminari; Ito, Hironobu; Tsumuraya, Yoichi; Kotake, Toshihisa

doi:10.1016/j.carres.2018.07.004

Cited by 14 publications

(7 citation statements)

References 30 publications

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“…The presence of either single and/or multiple AGP or FAS1 domains in FLAs opens the potential for a range of putative interactions, similar to that which occurs in mammalian FAS1 proteins. Support for some FLAs being glycosylated with AG glycans was shown by their interaction with β-glucosyl Yariv reagent that selectively precipitates AGPs (Johnson et al, 2003;Sato et al, 2018). Immunoprecipitation of Arabidopsis FLA4 showed it can be labeled with AGP-specific antibodies and is observed at a higher molecular weight than predicted by the protein backbone alone (Xue et al, 2017).…”

Section: Introductionmentioning

confidence: 99%

Fasciclin-Like Arabinogalactan-Protein 16 (FLA16) Is Required for Stem Development in Arabidopsis

et al. 2020

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The predominant Fascilin 1 (FAS1)-containing proteins in plants belong to the Fasciclin-Like Arabinogalactan-protein (FLA) family of extracellular glycoproteins. In addition to FAS1 domains, these multi-domain FLA proteins contain glycomotif regions predicted to direct addition of large arabinogalactan (AG) glycans and many contain signal sequences for addition of a glycosylphosphatidylinositol (GPI)-anchor to tether them to the plasma membrane. FLAs are proposed to play both structural and signaling functions by forming a range of interactions in the plant extracellular matrix, similar to FAS1-containing proteins in animals. FLA group B members contain two FAS1 domains and are not predicted to be GPI-anchored. None of the group B members have been functionally characterized or their sub-cellular location resolved, limiting understanding of their function. We investigated the group B FLA16 in Arabidopsis that is predominantly expressed in inflorescence tissues. FLA16 is the most highly expressed FLA in the stem after Group A members FLA11 and FLA12 that are stem specific. A FLA16-YFP fusion protein driven by the endogenous putative FLA16 promoter in wild type background showed expression in cells with secondary cell walls, and FLA16 displayed characteristics of cell wall glycoproteins with moderate glycosylation. Investigation of a fla16 mutant showed loss of FLA16 leads to reduced stem length and altered biomechanical properties, likely as a result of reduced levels of cellulose. Immuno-labeling indicated support for FLA16 location to the plasma-membrane and (apoplastic) cell wall of interfascicular stem fiber cells. Together these results indicate FLA16, a two-FAS1 domain FLAs, plays a role in plant secondary cell wall synthesis and function.

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Section: Introductionmentioning

confidence: 99%

Fasciclin-Like Arabinogalactan-Protein 16 (FLA16) Is Required for Stem Development in Arabidopsis

et al. 2020

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“…2013, Sato et al. 2018). They also showed that while the presence of protein moiety is not required, the extent of β‐(1,6)‐galactan substitution affects the Yariv reagent reactivity.…”

Section: Discussionmentioning

confidence: 96%

“…2013, Sato et al. 2018). The higher β‐(1,6)‐galactan substitution could explain the loss of other AGP‐like glycoproteins after β‐ d ‐glucosyl Yariv purification.…”

Section: Discussionmentioning

confidence: 96%

Arabinogalactan‐like Glycoproteins from Ulva lactuca (Chlorophyta) Show Unique Features Compared to Land Plants AGPs

Přerovská

Henke²,

Bleha³

et al. 2021

Journal of Phycology

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Arabinogalactan proteins (AGPs) encompass a diverse group of plant cell wall proteoglycans, which play an essential role in plant development, signaling, plant‐microbe interactions, and many others. Although they are widely distributed throughout the plant kingdom and extensively studied, they remain largely unexplored in the lower plants, especially in seaweeds. Ulva species have high economic potential since various applications were previously described including bioremediation, biofuel production, and as a source of bioactive compounds. This article presents the first experimental confirmation of AGP‐like glycoproteins in Ulva species and provides a simple extraction protocol of Ulva lactuca AGP‐like glycoproteins, their partial characterization and unique comparison to scarcely described Solanum lycopersicum AGPs. The reactivity with primary anti‐AGP antibodies as well as Yariv reagent showed a great variety between Ulva lactuca and Solanum lycopersicum AGP‐like glycoproteins. While the amino acid analysis of the AGP‐like glycoproteins purified by the β‐d‐glucosyl Yariv reagent showed a similarity between algal and land plant AGP‐like glycoproteins, neutral saccharide analysis revealed unique glycosylation of the Ulva lactuca AGP‐like glycoproteins. Surprisingly, arabinose and galactose were not the most prevalent monosaccharides and the most outstanding was the presence of 3‐O‐methyl‐hexose, which has never been described in the AGPs. The exceptional structure of the Ulva lactuca AGP‐like glycoproteins implies a specialized adaptation to the marine environment and might bring new insight into the evolution of the plant cell wall.

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“…Recently arabinogalactan was detected in the high molecular weight dissolved organic matter (HMWDOM) and POM fraction using monoclonal antibodies during the algal spring bloom in the North Sea (Vidal-Melgosa et al 2021 ). This coincides with the high arabinose and galactose content of Phaeocystis spp., a haptophyte blooming in the North Sea (Alderkamp et al 2007 , Sato et al 2018 ). The antibody-based quantification also showed a decrease in arabinogalactan content towards the end of the spring bloom, suggesting a fast turnover of the compound—contrasting with the accumulation of fucose-containing sulfated polysaccharides (Vidal-Melgosa et al 2021 ).…”

Section: Introductionmentioning

confidence: 99%

Proteomic insight into arabinogalactan utilization by particle-associated Maribacter sp. MAR_2009_72

Kalenborn,

Zühlke,

Riedel

et al. 2024

FEMS Microbiology Ecology

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Arabinose and galactose are major, rapidly metabolized components of marine particulate and dissolved organic matter. In this study, we observed for the first time large microbiomes for the degradation of arabinogalactan and report a detailed investigation of arabinogalactan utilization by the flavobacterium Maribacter sp. MAR_2009_72. Cellular extracts hydrolysed arabinogalactan in vitro. Comparative proteomic analyses of cells grown on arabinogalactan, arabinose, galactose, and glucose revealed the expression of specific proteins in the presence of arabinogalactan, mainly glycoside hydrolases (GH). Extracellular glycan hydrolysis involved five alpha-l-arabinofuranosidases affiliating with glycoside hydrolase families 43 and 51, four unsaturated rhamnogalacturonylhydrolases (GH105) and a protein with a glycoside hydrolase family-like domain. We detected expression of three induced TonB-dependent SusC/D transporter systems, one SusC, and nine glycoside hydrolases with a predicted periplasmatic location. These are affiliated with the families GH3, GH10, GH29, GH31, GH67, GH78, and GH115. The genes are located outside of and within canonical polysaccharide utilization loci classified as specific for arabinogalactan, for galactose-containing glycans, and for arabinose-containing glycans. The breadth of enzymatic functions expressed in Maribacter sp. MAR_2009_72 as response to arabinogalactan from the terrestrial plant larch suggests that Flavobacteriia are main catalysts of the rapid turnover of arabinogalactans in the marine environment.

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Yariv reactivity of type II arabinogalactan from larch wood

Cited by 14 publications

References 30 publications

Fasciclin-Like Arabinogalactan-Protein 16 (FLA16) Is Required for Stem Development in Arabidopsis

Fasciclin-Like Arabinogalactan-Protein 16 (FLA16) Is Required for Stem Development in Arabidopsis

Arabinogalactan‐like Glycoproteins from Ulva lactuca (Chlorophyta) Show Unique Features Compared to Land Plants AGPs

Proteomic insight into arabinogalactan utilization by particle-associated Maribacter sp. MAR_2009_72

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