The diversity of glycan chains in jellyfish mucin of three Cubozoan species: the contrast in molecular evolution rates of the peptide chain and Glycans.

IF 3.4 3区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Glycobiology Pub Date : 2024-11-05 DOI:10.1093/glycob/cwae090
Takuma Kaneko, Shinra Tanaka, Minami Sugiyama, Shiori Kaise, Hiroshi Inui, Kiminori Ushida
{"title":"The diversity of glycan chains in jellyfish mucin of three Cubozoan species: the contrast in molecular evolution rates of the peptide chain and Glycans.","authors":"Takuma Kaneko, Shinra Tanaka, Minami Sugiyama, Shiori Kaise, Hiroshi Inui, Kiminori Ushida","doi":"10.1093/glycob/cwae090","DOIUrl":null,"url":null,"abstract":"<p><p>The O-glycan composition of jellyfish (JF) mucin (qniumucin: Q-mucin) extracted from three Cubozoan species was studied after the optimization of the purification protocol. Application of a stepwise gradient of ionic strength to anion exchange chromatography (AEXC) was effective for isolating Q-mucin from coexisting impurities. In the three species, the amino acid sequence of the tandem repeat (TR) region in Q-mucin in all three Cubozoans seemed to remain the same as that in all Scyphozoans, although their glycan chains seemed to exhibit clear diversity. In particular, the amounts of acidic moieties on the glycan chains of Q-mucin from the Cubozoans markedly varied even in these genetically close species. In two of the three Cubozoan species, the fraction of disaccharides was large, showing a sharp contrast to that of the glycans of Q-mucin in Scyphozoans. This study also indicates that the simple sequence of TR commonly inherited in all Cubozoan and Scyphozoan JF species after the long term of evolution over 500 M years. According to this research, the glycans and the TR of mucin-type glycoproteins (MTGPs), forming a hierarchical structure, appear to complement each other in the evolutionary changes because the time required for their hereditary conversion is considerably different. The cooperation of these mechanisms is a strategy to achieve the contradictory functions of biosystems, namely species conservation and diversity acquisition.</p>","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.4000,"publicationDate":"2024-11-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Glycobiology","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1093/glycob/cwae090","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

The O-glycan composition of jellyfish (JF) mucin (qniumucin: Q-mucin) extracted from three Cubozoan species was studied after the optimization of the purification protocol. Application of a stepwise gradient of ionic strength to anion exchange chromatography (AEXC) was effective for isolating Q-mucin from coexisting impurities. In the three species, the amino acid sequence of the tandem repeat (TR) region in Q-mucin in all three Cubozoans seemed to remain the same as that in all Scyphozoans, although their glycan chains seemed to exhibit clear diversity. In particular, the amounts of acidic moieties on the glycan chains of Q-mucin from the Cubozoans markedly varied even in these genetically close species. In two of the three Cubozoan species, the fraction of disaccharides was large, showing a sharp contrast to that of the glycans of Q-mucin in Scyphozoans. This study also indicates that the simple sequence of TR commonly inherited in all Cubozoan and Scyphozoan JF species after the long term of evolution over 500 M years. According to this research, the glycans and the TR of mucin-type glycoproteins (MTGPs), forming a hierarchical structure, appear to complement each other in the evolutionary changes because the time required for their hereditary conversion is considerably different. The cooperation of these mechanisms is a strategy to achieve the contradictory functions of biosystems, namely species conservation and diversity acquisition.

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
三种腔肠动物的水母粘蛋白中糖链的多样性:肽链和糖的分子进化速度对比。
在对纯化方案进行优化后,研究了从三种腔肠动物中提取的水母粘蛋白(qniumucin:Q-mucin)的O-糖组成。阴离子交换色谱(AEXC)中离子强度梯度的应用可有效地将Q-粘蛋白从共存的杂质中分离出来。在这三种立方动物中,Q-粘蛋白中串联重复(TR)区的氨基酸序列似乎与所有镰刀动物中的氨基酸序列相同,但其糖链似乎表现出明显的多样性。特别是,即使在这些基因相近的物种中,立方动物 Q-粘蛋白糖链上酸性分子的数量也明显不同。在三个立方动物中的两个物种中,双糖的比例很大,这与镰刀动物 Q-粘蛋白的糖链形成了鲜明对比。这项研究还表明,经过 5 亿年的长期进化,TR 的简单序列在所有立方虫和球虫 JF 物种中普遍遗传。根据这项研究,粘蛋白型糖蛋白(MTGPs)的聚糖和TR形成了一个层次结构,在进化变化中似乎是相辅相成的,因为它们的遗传转化所需的时间大不相同。这些机制的合作是实现生物系统矛盾功能(即物种保护和多样性获取)的一种策略。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
Glycobiology
Glycobiology 生物-生化与分子生物学
CiteScore
7.50
自引率
4.70%
发文量
73
审稿时长
3 months
期刊介绍: Established as the leading journal in the field, Glycobiology provides a unique forum dedicated to research into the biological functions of glycans, including glycoproteins, glycolipids, proteoglycans and free oligosaccharides, and on proteins that specifically interact with glycans (including lectins, glycosyltransferases, and glycosidases). Glycobiology is essential reading for researchers in biomedicine, basic science, and the biotechnology industries. By providing a single forum, the journal aims to improve communication between glycobiologists working in different disciplines and to increase the overall visibility of the field.
期刊最新文献
A self-immolative Kdn-glycoside substrate enables high-throughput screening for inhibitors of Kdnases. Galectin-3 disrupts tight junctions of airway epithelial cell monolayers by inducing expression and release of matrix metalloproteinases upon influenza a infection. The 1st International Symposium on GPI and its Deficiency: Bridging Basic Research to Medical Frontiers in PNH and IGD. Why Nature Evolved GPI-anchored proteins: Unique Structure Characteristics Enable Versatile Cell Surface Functions. The diversity of glycan chains in jellyfish mucin of three Cubozoan species: the contrast in molecular evolution rates of the peptide chain and Glycans.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1