English  |  正體中文  |  简体中文  |  Items with full text/Total items : 54367/62174 (87%)
Visitors : 13946618      Online Users : 57
RC Version 6.0 © Powered By DSPACE, MIT. Enhanced by NTHU Library IR team.
Scope Tips:
  • please add "double quotation mark" for query phrases to get precise results
  • please goto advance search for comprehansive author search
  • Adv. Search
    HomeLoginUploadHelpAboutAdminister Goto mobile version
    National Tsing Hua University Institutional Repository > 生命科學院  > 生命科學系 > 期刊論文 >  Role of the linker region in the expression of Rhizopus oryzae glucoamylase


    Please use this identifier to cite or link to this item: http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/48954


    Title: Role of the linker region in the expression of Rhizopus oryzae glucoamylase
    Authors: Shu-Chuan Lin;Wei-Ting Liu;Shi-Hwei Liu;Wei-I Chou;Bor-Kai Hsiung;I-Ping Lin;Chia-Chin Sheu;Margaret Dah-Tsyr Chang
    教師: 張大慈
    Date: 2007
    Publisher: BioMed Central
    Relation: BMC Biochemistry,BioMed Central,Volume 8,Issue 9,2007
    Keywords: Rhizopus oryzae
    glucoamylase
    Abstract: Background
    Rhizopus oryzae glucoamylase (RoGA) consists of three domains: an amino (N)-terminal raw starch-binding domain (SBD), a glycosylated linker domain, and a carboxy (C)-terminal catalytic domain. The 36-amino-acid linker region (residues 132–167) connects the two functional domains, but its structural and functional roles are unclear.
    Results
    To characterize the linker sequences of RoGA and its involvement in protein expression, a number of RoGA variants containing deletions and mutations were constructed and expressed in Saccharomyces cerevisiae. Deletion analyses demonstrate that the linker region, especially within residues 161 to 167, is required for protein expression. In addition, site-directed mutagenesis and deglycosylation studies reveal that the linker region of RoGA contains both N- and O-linked carbohydrate moieties, and the N-linked oligosaccharides play a major role in the formation of active enzyme. Although the linker segment itself appears to have no ordered secondary structural conformation, the flexible region indeed contributes to the stabilization of functional N- and C-terminal domains.
    Conclusion
    Our data provide direct evidence that the length, composition, and glycosylation of the interdomain linker play a central role in the structure and function of RoGA.
    URI: http://www.biomedcentral.com/
    http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/48954
    Appears in Collections:[生命科學系] 期刊論文

    Files in This Item:

    File Description SizeFormat
    index.html0KbHTML329View/Open


    在NTHUR中所有的資料項目都受到原著作權保護,僅提供學術研究及教育使用,敬請尊重著作權人之權益。若須利用於商業或營利,請先取得著作權人授權。
    若發現本網站收錄之內容有侵害著作權人權益之情事,請權利人通知本網站管理者(smluo@lib.nthu.edu.tw),管理者將立即採取移除該內容等補救措施。

    SFX Query

    與系統管理員聯絡

    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback