5fv5
KpFlo11 presents a novel member of the Flo11 family with a unique recognition pattern for homophilic interactionsKpFlo11 presents a novel member of the Flo11 family with a unique recognition pattern for homophilic interactions
Structural highlights
FunctionFLO11_KOMPG Homophilic binding protein that enables kin discrimination in heterogeneous yeast populations by mediating homotypic cell-cell interactions during flocculation, a reversible and asexual process in which cells adhere to form aggregates (flocs).[1] Publication Abstract from PubMedMicroorganisms have evolved specific cell surface molecules that enable discrimination between cells from the same and from a different kind. Here, we investigate the role of Flo11-type cell surface adhesins from social yeasts in kin discrimination. We measure the adhesion forces mediated by Flo11A-type domains using single-cell force spectroscopy, quantify Flo11A-based cell aggregation in populations and determine the Flo11A-dependent segregation of competing yeast strains in biofilms. We find that Flo11A domains from diverse yeast species confer remarkably strong adhesion forces by establishing homotypic interactions between single cells, leading to efficient cell aggregation and biofilm formation in homogenous populations. Heterotypic interactions between Flo11A domains from different yeast species or Saccharomyces cerevisiae strains confer weak adhesive forces and lead to efficient strain segregation in heterogenous populations, indicating that in social yeasts Flo11A-mediated cell adhesion is a major mechanism for kin discrimination at species and sub-species levels. These findings, together with our structure and mutation analysis of selected Flo11A domains, provide a rationale of how cell surface receptors have evolved in microorganisms to mediate kin discrimination. Kin discrimination in social yeast is mediated by cell surface receptors of the Flo11 adhesin family.,Bruckner S, Schubert R, Kraushaar T, Hartmann R, Hoffmann D, Jelli E, Drescher K, Muller DJ, Oliver Essen L, Mosch HU Elife. 2020 Apr 14;9. pii: 55587. doi: 10.7554/eLife.55587. PMID:32286952[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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