Assembling the core protein complex of RNA processing events

M. Sobti, P. A. Haynes, G. Kornfeld, B. C. Mabbutt

    Research output: Contribution to journalMeeting abstract


    The LSm proteins are known to organize as multiprotein ring assemblies which interact with RNAs to allow chemical modification or nuclease protection. The determination of structures of large heterogenous protein complexes poses particular difficulty for structural biologists, requiring the careful assembly of components into a viable complex suitable for data collection. Avenues for in vitro assembly include recombinant construction of all or some components via co expression, or expression of polyproteins with engineered linkers. We describe our polyprotein construction of appropriate dimer, trimer and heptamer combinations known to make up mixed LSm subcomplexes. By reconstituting mixed complexes of LSms we are defining the heteroheptameric ring assemblies by crystallography and studying their specific interactions their associated protein factors.
    Original languageEnglish
    Pages (from-to)166
    Number of pages1
    JournalComBio 2006 : combined conference abstracts
    Publication statusPublished - 2006
    EventComBio2006 Conference - Brisbane
    Duration: 24 Sep 200628 Sep 2006


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