Arabinogalactan Structures of Repetitive Serine-Hydroxyproline Glycomodule Expressed by Arabidopsis Cell Suspension Cultures
Arabinogalactan-proteins (AGPs) are members of the hydroxyproline-rich glycoprotein (HRGP) superfamily. They are heavily glycosylated with arabinogalactans, which are usually composed of a β-1,3-linked galactan backbone with 6-<i>O</i>-linked galactosyl, oligo-1,6-galactosyl, or 1,6-gala...
| 出版年: | Plants |
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| 主要な著者: | , , , , |
| フォーマット: | 論文 |
| 言語: | 英語 |
| 出版事項: |
MDPI AG
2023-02-01
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| 主題: | |
| オンライン・アクセス: | https://www.mdpi.com/2223-7747/12/5/1036 |
| _version_ | 1851919932871147520 |
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| author | Li Tan Jianfeng Xu Michael Held Derek T. A. Lamport Marcia Kieliszewski |
| author_facet | Li Tan Jianfeng Xu Michael Held Derek T. A. Lamport Marcia Kieliszewski |
| author_sort | Li Tan |
| collection | DOAJ |
| container_title | Plants |
| description | Arabinogalactan-proteins (AGPs) are members of the hydroxyproline-rich glycoprotein (HRGP) superfamily. They are heavily glycosylated with arabinogalactans, which are usually composed of a β-1,3-linked galactan backbone with 6-<i>O</i>-linked galactosyl, oligo-1,6-galactosyl, or 1,6-galactan side chains that are further decorated with arabinosyl, glucuronosyl, rhamnosyl, and/or fucosyl residues. Here, our work with Hyp-<i>O</i>-polysaccharides isolated from (Ser-Hyp)<sub>32</sub>-EGFP (enhanced green fluorescent protein) fusion glycoproteins overexpressed in transgenic Arabidopsis suspension culture is consistent with the common structural features of AGPs isolated from tobacco. In addition, this work confirms the presence of β-1,6-linkage on the galactan backbone identified previously in AGP fusion glycoproteins expressed in tobacco suspension culture. Furthermore, the AGPs expressed in Arabidopsis suspension culture lack terminal-rhamnosyl residues and have a much lower level of glucuronosylation compared with those expressed in tobacco suspension culture. These differences not only suggest the presence of distinct glycosyl transferases for AGP glycosylation in the two systems, but also indicate the existence of minimum AG structures for type II AG functional features. |
| format | Article |
| id | doaj-art-80ce1983beb84b7d957f231dfd7cf352 |
| institution | Directory of Open Access Journals |
| issn | 2223-7747 |
| language | English |
| publishDate | 2023-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| spelling | doaj-art-80ce1983beb84b7d957f231dfd7cf3522025-08-19T21:58:42ZengMDPI AGPlants2223-77472023-02-01125103610.3390/plants12051036Arabinogalactan Structures of Repetitive Serine-Hydroxyproline Glycomodule Expressed by Arabidopsis Cell Suspension CulturesLi Tan0Jianfeng Xu1Michael Held2Derek T. A. Lamport3Marcia Kieliszewski4Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30602, USAArkansas Biosciences Institute, Arkansas State University, Jonesboro, AR 72401, USADepartment of Chemistry and Biochemistry, Ohio University, Athens, OH 45701, USASchool of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG, UKDepartment of Chemistry and Biochemistry, Ohio University, Athens, OH 45701, USAArabinogalactan-proteins (AGPs) are members of the hydroxyproline-rich glycoprotein (HRGP) superfamily. They are heavily glycosylated with arabinogalactans, which are usually composed of a β-1,3-linked galactan backbone with 6-<i>O</i>-linked galactosyl, oligo-1,6-galactosyl, or 1,6-galactan side chains that are further decorated with arabinosyl, glucuronosyl, rhamnosyl, and/or fucosyl residues. Here, our work with Hyp-<i>O</i>-polysaccharides isolated from (Ser-Hyp)<sub>32</sub>-EGFP (enhanced green fluorescent protein) fusion glycoproteins overexpressed in transgenic Arabidopsis suspension culture is consistent with the common structural features of AGPs isolated from tobacco. In addition, this work confirms the presence of β-1,6-linkage on the galactan backbone identified previously in AGP fusion glycoproteins expressed in tobacco suspension culture. Furthermore, the AGPs expressed in Arabidopsis suspension culture lack terminal-rhamnosyl residues and have a much lower level of glucuronosylation compared with those expressed in tobacco suspension culture. These differences not only suggest the presence of distinct glycosyl transferases for AGP glycosylation in the two systems, but also indicate the existence of minimum AG structures for type II AG functional features.https://www.mdpi.com/2223-7747/12/5/1036arabinogalactan-proteinsarabinogalactan polysaccharidesglycosylationNMR |
| spellingShingle | Li Tan Jianfeng Xu Michael Held Derek T. A. Lamport Marcia Kieliszewski Arabinogalactan Structures of Repetitive Serine-Hydroxyproline Glycomodule Expressed by Arabidopsis Cell Suspension Cultures arabinogalactan-proteins arabinogalactan polysaccharides glycosylation NMR |
| title | Arabinogalactan Structures of Repetitive Serine-Hydroxyproline Glycomodule Expressed by Arabidopsis Cell Suspension Cultures |
| title_full | Arabinogalactan Structures of Repetitive Serine-Hydroxyproline Glycomodule Expressed by Arabidopsis Cell Suspension Cultures |
| title_fullStr | Arabinogalactan Structures of Repetitive Serine-Hydroxyproline Glycomodule Expressed by Arabidopsis Cell Suspension Cultures |
| title_full_unstemmed | Arabinogalactan Structures of Repetitive Serine-Hydroxyproline Glycomodule Expressed by Arabidopsis Cell Suspension Cultures |
| title_short | Arabinogalactan Structures of Repetitive Serine-Hydroxyproline Glycomodule Expressed by Arabidopsis Cell Suspension Cultures |
| title_sort | arabinogalactan structures of repetitive serine hydroxyproline glycomodule expressed by arabidopsis cell suspension cultures |
| topic | arabinogalactan-proteins arabinogalactan polysaccharides glycosylation NMR |
| url | https://www.mdpi.com/2223-7747/12/5/1036 |
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