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dc.contributor.authorGu, Shuang
dc.description.abstractThe type II secretion system (T2SS) is the major terminal branch of the general secretory pathway. It is composed of 12-15 proteins, most in multiple copies, and spans the inner and outer membranes of Gram-negative bacteria. The T2SS secretin subunits form a large dodecameric torus-like structure in the outer membrane. The secretin is the only essential component in the outer membrane and secreted proteins and virulence factors pass through the pore in the toroidal secretin dodecamer and out into the environment. The interaction between the secretin and its partners plays a key role in regulation of the T2SS. The interaction between the so-called homology region of the innermembrane protein GspC (GspC-HR) and secretin provides the structural and functional integrity of the secretion machinery across the two cell membranes. The interaction between secretin and its pilotin translocates the secretin subunits to the outer membrane. In this Thesis, the interactions between secretin and its partners are studied at molecular level. The GspC-HR structure is solved using NMR spectroscopy. Its interaction with secretin (GspD) is elucidated using several biochemical and biophysical approaches and a model of the complex is proposed. Also, the interaction between secretin (GspD) and pilotin (GspS) is further charicterisied. An 18 residues secretin sequence is identified as responsible for interacting with pilotin. Upon binding to the pilotin, the unstructured secretin forms a helical structure.en_US
dc.description.sponsorshipMRC NMR centre (NIMR), Medical Research Council
dc.description.sponsorshipNational Institute for Medical Research (NIMR) N.M.R. Centre
dc.publisherQueen Mary University of London
dc.subjectsynthetic bone graften_US
dc.subjectmaterial propertiesen_US
dc.subjectprotein adsorptionen_US
dc.subjectcell attachment, proliferation and differentiationen_US
dc.subjectserum protein interactionsen_US
dc.subjectstrut porosityen_US
dc.titleSecretin interactions in the type II secretion systemen_US
dc.rights.holderThe copyright of this thesis rests with the author and no quotation from it or information derived from it may be published without the prior written consent of the author

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  • Theses [3371]
    Theses Awarded by Queen Mary University of London

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