Arabinogalactan Structures of Repetitive Serine-Hydroxyproline Glycomodule Expressed by Arabidopsis Cell Suspension Cultures.
Arabinogalactan Structures of Repetitive Serine-Hydroxyproline Glycomodule Expressed by Arabidopsis Cell Suspension Cultures.
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DOI：
10.3390/plants12051036
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发表时间：
2023-02-24
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影响因子：
--
通讯作者：
Kieliszewski M
中科院分区：
文献类型：
--
作者：
Tan L;Xu J;Held M;Lamport DTA;Kieliszewski M
阿拉伯半乳聚糖蛋白（AGPs）是富含羟脯氨酸的糖蛋白（HRGP）超家族的成员。它们被阿拉伯半乳聚糖高度糖基化，阿拉伯半乳聚糖通常由β-1，3-连接的半乳聚糖主链和6-O-连接的半乳糖基、寡-1，6-半乳糖基或1，6-半乳聚糖侧链组成，这些侧链进一步被阿拉伯糖基、葡糖醛酸基、鼠李糖基和/或岩藻糖基残基修饰。在这里，我们的工作与Hyp-O-多糖分离的（Ser-Hyp）32-EGFP（增强型绿色荧光蛋白）融合糖蛋白在转基因拟南芥悬浮培养物中过表达是一致的，从烟草中分离的AGP的共同结构特征。此外，这项工作证实了在烟草悬浮培养物中表达的AGP融合糖蛋白中先前鉴定的半乳聚糖骨架上存在β-1，6-键。此外，在拟南芥悬浮培养中表达的AGP缺乏末端-鼠李糖残基，并且与在烟草悬浮培养中表达的AGP相比具有低得多的葡萄糖醛酸基化水平。这些差异不仅表明存在不同的糖基转移酶的AGP糖基化在两个系统中，但也表明存在最低AG结构的II型AG功能的特点。
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-O-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-O-polysaccharides isolated from (Ser-Hyp)32-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.
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