QIBEBT-IR  > 微生物代谢工程研究组
CELLULOSE SYNTHASE-LIKE A2, a Glucomannan Synthase, Is Involved in Maintaining Adherent Mucilage Structure in Arabidopsis Seed(1[C][W])
Yu, Li1; Shi, Dachuan1,2; Li, Junling1,2; Kong, Yingzhen3; Yu, Yanchong1; Chai, Guohua1; Hu, Ruibo1; Wang, Juan1; Hahn, Michael G.4; Zhou, Gongke1
2014-04-01
发表期刊PLANT PHYSIOLOGY
卷号164期号:4页码:1842-1856
摘要

Mannans are hemicellulosic polysaccharides that are considered to have both structural and storage functions in the plant cell wall. However, it is not yet known how mannans function in Arabidopsis (Arabidopsis thaliana) seed mucilage. In this study, CELLULOSE SYNTHASE-LIKE A2 (CSLA2; At5g22740) expression was observed in several seed tissues, including the epidermal cells of developing seed coats. Disruption of CSLA2 resulted in thinner adherent mucilage halos, although the total amount of the adherent mucilage did not change compared with the wild type. This suggested that the adherent mucilage in the mutant was more compact compared with that of the wild type. In accordance with the role of CSLA2 in glucomannan synthesis, csla2-1 mucilage contained 30% less mannosyl and glucosyl content than did the wild type. No appreciable changes in the composition, structure, or macromolecular properties were observed for nonmannan polysaccharides in mutant mucilage. Biochemical analysis revealed that cellulose crystallinity was substantially reduced in csla2-1 mucilage; this was supported by the removal of most mucilage cellulose through treatment of csla2-1 seeds with endo-beta-glucanase. Mutation in CSLA2 also resulted in altered spatial distribution of cellulose and an absence of birefringent cellulose microfibrils within the adherent mucilage. As with the observed changes in crystalline cellulose, the spatial distribution of pectin was also modified in csla2-1 mucilage. Taken together, our results demonstrate that glucomannans synthesized by CSLA2 are involved in modulating the structure of adherent mucilage, potentially through altering cellulose organization and crystallization.

文章类型Article
WOS标题词Science & Technology ; Life Sciences & Biomedicine
DOI10.1104/pp.114.236596
关键词[WOS]SEED COAT MUCILAGE ; PLANT-CELL WALL ; MONOCLONAL-ANTIBODIES ; TRANSCRIPTION FACTOR ; SECRETORY-CELLS ; EPIDERMAL-CELLS ; FAMILY-MEMBERS ; IN-SITU ; THALIANA ; GENE
收录类别SCI
语种英语
WOS研究方向Plant Sciences
WOS类目Plant Sciences
WOS记录号WOS:000334342800026
引用统计
文献类型期刊论文
条目标识符http://ir.qibebt.ac.cn/handle/337004/6276
专题微生物代谢工程研究组
作者单位1.Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Shandong Prov Key Lab Energy Genet, Key Lab Biofuels, Qingdao 266101, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
3.Chinese Acad Agr Sci, Tobacco Res Inst, Key Lab Tobacco Gene Resources, Qingdao, Peoples R China
4.Univ Georgia, Complex Carbohydrate Res Ctr, Athens, GA 30602 USA
推荐引用方式
GB/T 7714
Yu, Li,Shi, Dachuan,Li, Junling,et al. CELLULOSE SYNTHASE-LIKE A2, a Glucomannan Synthase, Is Involved in Maintaining Adherent Mucilage Structure in Arabidopsis Seed(1[C][W])[J]. PLANT PHYSIOLOGY,2014,164(4):1842-1856.
APA Yu, Li.,Shi, Dachuan.,Li, Junling.,Kong, Yingzhen.,Yu, Yanchong.,...&Zhou, Gongke.(2014).CELLULOSE SYNTHASE-LIKE A2, a Glucomannan Synthase, Is Involved in Maintaining Adherent Mucilage Structure in Arabidopsis Seed(1[C][W]).PLANT PHYSIOLOGY,164(4),1842-1856.
MLA Yu, Li,et al."CELLULOSE SYNTHASE-LIKE A2, a Glucomannan Synthase, Is Involved in Maintaining Adherent Mucilage Structure in Arabidopsis Seed(1[C][W])".PLANT PHYSIOLOGY 164.4(2014):1842-1856.
条目包含的文件 下载所有文件
文件名称/大小 文献类型 版本类型 开放类型 使用许可
CELLULOSE SYNTHASE-L(1398KB)期刊论文作者接受稿开放获取CC BY-NC-SA浏览 下载
个性服务
推荐该条目
保存到收藏夹
查看访问统计
导出为Endnote文件
谷歌学术
谷歌学术中相似的文章
[Yu, Li]的文章
[Shi, Dachuan]的文章
[Li, Junling]的文章
百度学术
百度学术中相似的文章
[Yu, Li]的文章
[Shi, Dachuan]的文章
[Li, Junling]的文章
必应学术
必应学术中相似的文章
[Yu, Li]的文章
[Shi, Dachuan]的文章
[Li, Junling]的文章
相关权益政策
暂无数据
收藏/分享
文件名: CELLULOSE SYNTHASE-LIKE A2, a Glucomannan Synthase, Is Involved in Maintaining Adherent Mucilage Structure in Arabidopsis Seed.pdf
格式: Adobe PDF
此文件暂不支持浏览
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。