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  • Mechanism of Oligomerisation of Cyclase-associated Protein from Dictyostelium discoideum in Solution

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    Author(s)
    Yusof, Adlina Mohd
    Jaenicke, Elmar
    Pedersen, Jan Skov
    Noegel, Angelika A
    Schleicher, Michael
    Hofmann, Andreas
    Griffith University Author(s)
    Hofmann, Andreas
    Year published
    2006
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    Abstract
    Cyclase-associated protein (CAP) is a highly conserved modular protein implicated in the regulation of actin filament dynamics and a variety of developmental and morphological processes. The protein exists as a high molecular weight complex in cell extracts and purified protein possesses a high tendency to aggregate, a major obstacle for crystallisation. Using a mutagenesis approach, we show that two structural features underlie the mechanism of oligomerisation in Dictyostelium discoideum CAP. Positively charged clusters on the surface of the N-terminal helix-barrel domain are involved in inter-molecular interactions with ...
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    Cyclase-associated protein (CAP) is a highly conserved modular protein implicated in the regulation of actin filament dynamics and a variety of developmental and morphological processes. The protein exists as a high molecular weight complex in cell extracts and purified protein possesses a high tendency to aggregate, a major obstacle for crystallisation. Using a mutagenesis approach, we show that two structural features underlie the mechanism of oligomerisation in Dictyostelium discoideum CAP. Positively charged clusters on the surface of the N-terminal helix-barrel domain are involved in inter-molecular interactions with the N or C-terminal domains. Abolishing these interactions mainly renders dimers due to a domain swap feature in the extreme C-terminal region of the protein that was previously described. Based on earlier studies with yeast CAP, we also generated constructs with mutations in the extreme N-terminal region of Dictyostelium CAP that did not show significantly altered oligomerisation behaviour. Constructs with mutations in the earlier identified protein-protein interaction interface on the N-terminal domain of CAP could not be expressed as soluble protein. Assessment of the soluble proteins indicates that the mutations did not affect their overall fold. Further studies point to the correlation between stability of full-length CAP with its multimerisation behaviour, where oligomer formation leads to a more stable protein.
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    Journal Title
    Journal of Molecular Biology
    Volume
    362
    DOI
    https://doi.org/10.1016/j.jmb.2006.08.008
    Copyright Statement
    © 2006 Elsevier. This is the author-manuscript version of this paper. Reproduced in accordance with the copyright policy of the publisher. Please refer to the journal's website for access to the definitive, published version.
    Subject
    Medicinal and biomolecular chemistry
    Biochemistry and cell biology
    Microbiology
    Publication URI
    http://hdl.handle.net/10072/15562
    Collection
    • Journal articles

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