Association between the intrinsically disordered protein PEX19 and PEX3

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dc.contributor Aalto-yliopisto fi
dc.contributor Aalto University en
dc.contributor.author Hattula, K.
dc.contributor.author Hirschberg, D.
dc.contributor.author Kalkkinen, N.
dc.contributor.author Butcher, S.J.
dc.contributor.author Ora, A.
dc.date.accessioned 2017-05-11T06:55:00Z
dc.date.available 2017-05-11T06:55:00Z
dc.date.issued 2014
dc.identifier.citation Hattula , K , Hirschberg , D , Kalkkinen , N , Butcher , S J & Ora , A 2014 , ' Association between the intrinsically disordered protein PEX19 and PEX3 ' PLOS ONE , vol 9 , no. 7 , e103101 , pp. 1-10 . DOI: 10.1371/journal.pone.0103101 en
dc.identifier.issn 1932-6203
dc.identifier.other PURE UUID: 453184db-0a68-4024-951a-a61a9edd93e2
dc.identifier.other PURE ITEMURL: https://research.aalto.fi/en/publications/association-between-the-intrinsically-disordered-protein-pex19-and-pex3(453184db-0a68-4024-951a-a61a9edd93e2).html
dc.identifier.other PURE LINK: http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0103101
dc.identifier.other PURE FILEURL: https://research.aalto.fi/files/12864697/journal.pone.0103101.pdf
dc.identifier.uri https://aaltodoc.aalto.fi/handle/123456789/25487
dc.description.abstract In peroxisomes, peroxins (PEXs) 3 and 19 are the principal protein components of the machinery required for early peroxisomal biogenesis. For further insight into the interaction of PEX3 and PEX19, we used hydrogen exchange mass spectrometry to monitor conformational changes during complex formation between PEX3 and PEX19 in vitro. Our data showed that PEX19 remained highly flexible during interaction with PEX3. However, we could detect three changes, one each in the N-and C-terminus along with a small stretch in the middle of PEX19 (F64–L74) which became shielded from hydrogen exchange when interacting with PEX3. PEX3 became more protected from hydrogen exchange in the binding groove for PEX19 with only small changes elsewhere. Most likely the N-terminus of PEX19 initiates the binding to PEX3, and then subtle conformational changes in PEX3 affect the surface of the PEX3 molecule. PEX19 in turn, is stabilized by folding of a short helix and its C-terminal folding core permitting PEX19 to bind to PEX3 with higher affinity than just the N-terminal interaction allows. Thus within the cell, PEX3 is stabilized by PEX19 preventing PEX3 aggregation. en
dc.format.extent 1-10
dc.format.mimetype application/pdf
dc.language.iso en en
dc.relation.ispartofseries PLOS ONE en
dc.relation.ispartofseries Volume 9, issue 7 en
dc.rights openAccess en
dc.subject.other 114 Physical sciences en
dc.subject.other 221 Nanotechnology en
dc.subject.other 214 Mechanical engineering en
dc.subject.other 218 Environmental engineering en
dc.title Association between the intrinsically disordered protein PEX19 and PEX3 en
dc.type A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä fi
dc.description.version Peer reviewed en
dc.contributor.department Department of Applied Physics
dc.subject.keyword disordered protein
dc.subject.keyword hydrogen exchange
dc.subject.keyword mass spectrometry
dc.subject.keyword peroxin
dc.subject.keyword 114 Physical sciences
dc.subject.keyword 221 Nanotechnology
dc.subject.keyword 214 Mechanical engineering
dc.subject.keyword 218 Environmental engineering
dc.identifier.urn URN:NBN:fi:aalto-201705113871
dc.identifier.doi 10.1371/journal.pone.0103101
dc.type.version publishedVersion


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