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  • 1
    UID:
    b3kat_BV037217042
    Format: 1 Online-Ressource (123 S.) , Ill., graph. Darst.
    Note: Berlin, Humboldt-Univ., Diss., 2011
    Language: English
    Subjects: Biology
    RVK:
    Keywords: Hochschulschrift
    URL: Volltext  (kostenfrei)
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    UID:
    b3kat_BV037252595
    Format: X, 112 S. , Ill., graph. Darst.
    Note: Berlin, Humboldt-Univ., Diss., 2011
    Language: English
    Subjects: Biology
    RVK:
    Keywords: Hochschulschrift
    Library Location Call Number Volume/Issue/Year Availability
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  • 3
    Book
    Book
    wu han
    UID:
    gbv_1035697645
    Format: 2, 2, 294 S.
    Original writing title: 中国高校自主招生研究
    Original writing person/organisation: 樊本富
    Original writing publisher: 武汉 : 华中师范大学出版社
    ISBN: 9787562247142
    Series Statement: gao kao gai ge yan jiu cong shu
    Note: 有附录、附参考文献 , SBB-PK Berlin
    Language: Chinese
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  • 4
    Book
    Book
    bei jing
    UID:
    gbv_1037902173
    Format: 1 册
    Original writing title: 非洲地质图 : = An outline of the geology of Africa
    Original writing person/organisation: 楚旭春
    Original writing publisher: 北京 : 地图出版社
    Note: SBB-PK Berlin
    Language: Chinese
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  • 5
    UID:
    edochu_18452_24003
    Format: 1 Online-Ressource (15 Seiten)
    Content: S-ribosylhomocysteine lyase (LuxS) has been shown to regulate bacterial multicellular behaviors, typically biofilm formation. However, the mechanisms for the regulation are still mysterious. We previously identified a malonylation modification on K124 and K130 of the LuxS in the plant growth-promoting rhizobacterium B. velezensis (FZB42). In this work, we investigated the effects of the two malonylation sites on biofilm formation and other biological characteristics of FZB42. The results showed that the K124R mutation could severely impair biofilm formation, swarming, and sporulation but promote AI-2 production, suggesting inhibitory effects of high-level AI-2 on the features. All mutations (K124R, K124E, K130R, and K130E) suppressed FZB42 sporulation but increased its antibiotic production. The double mutations generally had a synergistic effect or at least equal to the effects of the single mutations. The mutation of K130 but not of K124 decreased the in vitro enzymatic activity of LuxS, corresponding to the conservation of K130 among various Bacillus LuxS proteins. From the results, we deduce that an alternative regulatory circuit may exist to compensate for the roles of LuxS upon its disruption. This study broadens the understanding of the biological function of LuxS in bacilli and underlines the importance of the two post-translational modification sites.
    Content: Peer Reviewed
    In: Basel : MDPI, 9,6
    Language: English
    URL: Volltext  (kostenfrei)
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