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dc.contributor.authorYusof, Adlina Mohd
dc.contributor.authorJaenicke, Elmar
dc.contributor.authorPedersen, Jan Skov
dc.contributor.authorNoegel, Angelika A
dc.contributor.authorSchleicher, Michael
dc.contributor.authorHofmann, Andreas
dc.date.accessioned2017-05-03T15:19:27Z
dc.date.available2017-05-03T15:19:27Z
dc.date.issued2006
dc.identifier.issn0022-2836
dc.identifier.doi10.1016/j.jmb.2006.08.008
dc.identifier.urihttp://hdl.handle.net/10072/15562
dc.description.abstractCyclase-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.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.format.extent2517175 bytes
dc.format.extent45217 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.languageEnglish
dc.language.isoeng
dc.publisherElsevier
dc.publisher.placeNew Jersey
dc.relation.ispartofstudentpublicationY
dc.relation.ispartofpagefrom1072
dc.relation.ispartofpageto1081
dc.relation.ispartofjournalJournal of Molecular Biology
dc.relation.ispartofvolume362
dc.rights.retentionY
dc.subject.fieldofresearchMedicinal and biomolecular chemistry
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchMicrobiology
dc.subject.fieldofresearchcode3404
dc.subject.fieldofresearchcode3101
dc.subject.fieldofresearchcode3107
dc.titleMechanism of Oligomerisation of Cyclase-associated Protein from Dictyostelium discoideum in Solution
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.rights.copyright© 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.
gro.date.issued2015-05-06T03:04:39Z
gro.hasfulltextFull Text
gro.griffith.authorHofmann, Andreas


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