Sequence characteristics responsible for protein-protein interactions in the intrinsically disordered regions of caseins, amelogenins, and small heat-shock proteins

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dc.contributor.authorHolt, Carl
dc.contributor.authorRaynes, J. K.
dc.contributor.authorCarver, John
dc.date.accessioned2020-03-19T04:15:17Z
dc.date.issued2019
dc.date.updated2019-11-25T07:43:25Z
dc.description.abstractMilk caseins and dental amelogenins are intrinsically disordered proteins (IDPs) that associate with themselves and others. Paradoxically, they are also described as hydrophobic proteins, which is difficult to reconcile with a solvent-exposed conformation. We attempt to resolve this paradox. We show that caseins and amelogenins are not hydrophobic proteins but they are more hydrophobic than most IDPs. Remarkably, uncharged residues from different regions of these mature proteins have a nearly constant average hydropathy but these regions exhibit different charged residue frequencies. A novel sequence analysis method was developed to identify hydrophobic and order-promoting regions that would favor conformational collapse. We found that such regions were uncommon; most hydrophobic and order-promoting residues were adjacent to hydrophilic or disorder-promoting residues. A further reason why caseins and amelogenins do not collapse is their high proportion of disorder-promoting proline residues. We conclude that in these proteins the hydrophobic effect is not large enough to cause conformational collapse but it can contribute, along with polar interactions, to protein-protein interactions. This behaviour is similar to the interaction of the disordered N-terminal region of small heat-shock proteins with either themselves during oligomer formation or other, unfolding, proteins during chaperone action.en_AU
dc.description.sponsorshipJC's research was supported by a grant (#1068087) from the National Health and Medical Research Council of Australia.en_AU
dc.format.mimetypeapplication/pdfen_AU
dc.identifier.citationHolt C, Raynes JK, Carver JA. Sequence characteristics responsible for protein-protein interactions in the intrinsically disordered regions of caseins, amelogenins, and small heat-shock proteins. Biopolymers. 2019;110:e23319. https://doi.org/10.1002/bip.23319en_AU
dc.identifier.issn0006-3525en_AU
dc.identifier.urihttp://hdl.handle.net/1885/202383
dc.language.isoen_AUen_AU
dc.publisherJohn Wiley & Sons Incen_AU
dc.relationhttp://purl.org/au-research/grants/nhmrc/1068087en_AU
dc.rights© 2019 Wiley Periodicals, Inc.en_AU
dc.sourceBiopolymersen_AU
dc.subjectamelogeninen_AU
dc.subjectcaseinen_AU
dc.subjectheat-shock proteinen_AU
dc.subjecthydrophobic and hydrophilic interactionsen_AU
dc.subjectintrinsically disordered proteinen_AU
dc.titleSequence characteristics responsible for protein-protein interactions in the intrinsically disordered regions of caseins, amelogenins, and small heat-shock proteinsen_AU
dc.typeJournal articleen_AU
dcterms.dateAccepted2019-06-19
local.bibliographicCitation.issuee23319en_AU
local.bibliographicCitation.lastpage15en_AU
local.bibliographicCitation.startpage1en_AU
local.contributor.affiliationHolt, Carl, University of Glasgowen_AU
local.contributor.affiliationRaynes, J. K., CSIRO Food and Nutritionen_AU
local.contributor.affiliationCarver, John, College of Science, ANUen_AU
local.contributor.authoremailu1571001@anu.edu.auen_AU
local.contributor.authoruidCarver, John, u1571001en_AU
local.description.embargo2037-12-31
local.description.notesImported from ARIESen_AU
local.identifier.absfor030400 - MEDICINAL AND BIOMOLECULAR CHEMISTRYen_AU
local.identifier.ariespublicationu3102795xPUB4727en_AU
local.identifier.citationvolume110en_AU
local.identifier.doi10.1002/bip.23319en_AU
local.identifier.thomsonIDWOS:000477523600001
local.identifier.uidSubmittedByu3102795en_AU
local.publisher.urlhttps://onlinelibrary.wiley.com/en_AU
local.type.statusPublished Versionen_AU

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