Identification and molecular analysis of interaction sites in the MtSEO-F1 protein involved in forisome assembly

dc.bibliographicCitation.firstPage603eng
dc.bibliographicCitation.journalTitleInternational Journal of Biological Macromoleculeseng
dc.bibliographicCitation.lastPage614eng
dc.bibliographicCitation.volume144eng
dc.contributor.authorRose, Judith
dc.contributor.authorVisser, Franziska
dc.contributor.authorMüller, Boje
dc.contributor.authorSenft, Matthias
dc.contributor.authorGroscurth, Sira
dc.contributor.authorSicking, Kevin F.
dc.contributor.authorTwyman, Richard M.
dc.contributor.authorPrüfer, Dirk
dc.contributor.authorNoll, Gundula A.
dc.date.accessioned2021-07-23T06:09:00Z
dc.date.available2021-07-23T06:09:00Z
dc.date.issued2020
dc.description.abstractForisomes are large mechanoprotein complexes found solely in legumes such as Medicago truncatula. They comprise several “sieve element occlusion by forisome” (SEO-F) subunits, with MtSEO-F1 as the major structure-forming component. SEO-F proteins possess three conserved domains –an N-terminal domain (SEO-NTD), a potential thioredoxin fold, and a C-terminal domain (SEO-CTD)– but structural and biochemical data are scarce and little is known about the contribution of these domains to forisome assembly. To identify key amino acids involved in MtSEO-F1 dimerization and complex formation, we investigated protein-protein interactions by bimolecular fluorescence complementation and the analysis of yeast two-hybrid and random mutagenesis libraries. We identified a SEO-NTD core region as the major dimerization site, with abundant hydrophobic residues and rare charged residues suggesting dimerization is driven by the hydrophobic effect. We also found that ~45% of the full-length MtSEO-F1 sequence must be conserved for higher-order protein assembly, indicating that large interaction surfaces facilitate stable interactions, contributing to the high resilience of forisome bodies. Interestingly, the removal of 62 amino acids from the C-terminus did not disrupt forisome assembly. This is the first study unraveling interaction sites and mechanisms within the MtSEO-F1 protein at the level of dimerization and complex formation. © 2018eng
dc.description.versionpublishedVersioneng
dc.identifier.urihttps://oa.tib.eu/renate/handle/123456789/6322
dc.identifier.urihttps://doi.org/10.34657/5369
dc.language.isoengeng
dc.publisherNew York, NY [u.a.] : Elseviereng
dc.relation.doihttps://doi.org/10.1016/j.ijbiomac.2019.12.092
dc.relation.essn1879-0003
dc.relation.issn0141-8130
dc.rights.licenseCC BY-NC-ND 4.0 Unportedeng
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/eng
dc.subject.ddc540eng
dc.subject.ddc570eng
dc.subject.otherForisomeeng
dc.subject.otherHydrophobic interactioneng
dc.subject.otherProtein assemblyeng
dc.titleIdentification and molecular analysis of interaction sites in the MtSEO-F1 protein involved in forisome assemblyeng
dc.typeArticleeng
dc.typeTexteng
tib.accessRightsopenAccesseng
wgl.contributorATBeng
wgl.subjectBiowissensschaften/Biologieeng
wgl.typeZeitschriftenartikeleng
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