Identification and molecular analysis of interaction sites in the MtSEO-F1 protein involved in forisome assembly
dc.bibliographicCitation.firstPage | 603 | eng |
dc.bibliographicCitation.journalTitle | International Journal of Biological Macromolecules | eng |
dc.bibliographicCitation.lastPage | 614 | eng |
dc.bibliographicCitation.volume | 144 | eng |
dc.contributor.author | Rose, Judith | |
dc.contributor.author | Visser, Franziska | |
dc.contributor.author | Müller, Boje | |
dc.contributor.author | Senft, Matthias | |
dc.contributor.author | Groscurth, Sira | |
dc.contributor.author | Sicking, Kevin F. | |
dc.contributor.author | Twyman, Richard M. | |
dc.contributor.author | Prüfer, Dirk | |
dc.contributor.author | Noll, Gundula A. | |
dc.date.accessioned | 2021-07-23T06:09:00Z | |
dc.date.available | 2021-07-23T06:09:00Z | |
dc.date.issued | 2020 | |
dc.description.abstract | Forisomes 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. © 2018 | eng |
dc.description.version | publishedVersion | eng |
dc.identifier.uri | https://oa.tib.eu/renate/handle/123456789/6322 | |
dc.identifier.uri | https://doi.org/10.34657/5369 | |
dc.language.iso | eng | eng |
dc.publisher | New York, NY [u.a.] : Elsevier | eng |
dc.relation.doi | https://doi.org/10.1016/j.ijbiomac.2019.12.092 | |
dc.relation.essn | 1879-0003 | |
dc.relation.issn | 0141-8130 | |
dc.rights.license | CC BY-NC-ND 4.0 Unported | eng |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/4.0/ | eng |
dc.subject.ddc | 540 | eng |
dc.subject.ddc | 570 | eng |
dc.subject.other | Forisome | eng |
dc.subject.other | Hydrophobic interaction | eng |
dc.subject.other | Protein assembly | eng |
dc.title | Identification and molecular analysis of interaction sites in the MtSEO-F1 protein involved in forisome assembly | eng |
dc.type | Article | eng |
dc.type | Text | eng |
tib.accessRights | openAccess | eng |
wgl.contributor | ATB | eng |
wgl.subject | Biowissensschaften/Biologie | eng |
wgl.type | Zeitschriftenartikel | eng |
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