Yeast Cell Adhesion Molecules Have Functional Amyloid-Forming Sequences

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dc.contributor.author Khalaf, Roy A.
dc.contributor.author Ramsook, Caleen B.
dc.contributor.author Tan, Cho
dc.contributor.author Garcia, Melissa C.
dc.contributor.author Fung, Raymond
dc.contributor.author Soybelman, Gregory
dc.date.accessioned 2016-03-21T08:37:47Z
dc.date.available 2016-03-21T08:37:47Z
dc.date.copyright 2010
dc.date.issued 2016-03-21
dc.identifier.issn 1535-9778 en_US
dc.identifier.uri http://hdl.handle.net/10725/3369
dc.description.abstract The occurrence of highly conserved amyloid-forming sequences in Candida albicans Als proteins (H. N. Otoo et al., Eukaryot. Cell 7:776–782, 2008) led us to search for similar sequences in other adhesins from C. albicans and Saccharomyces cerevisiae. The β-aggregation predictor TANGO found highly β-aggregation-prone sequences in almost all yeast adhesins. These sequences had an unusual amino acid composition: 77% of their residues were β-branched aliphatic amino acids Ile, Thr, and Val, which is more than 4-fold greater than their prevalence in the S. cerevisiae proteome. High β-aggregation potential peptides from S. cerevisiae Flo1p and C. albicans Eap1p rapidly formed insoluble amyloids, as determined by Congo red absorbance, thioflavin T fluorescence, and fiber morphology. As examples of the amyloid-forming ability of the native proteins, soluble glycosylphosphatidylinositol (GPI)-less fragments of C. albicans Als5p and S. cerevisiae Muc1p also formed amyloids within a few days under native conditions at nM concentrations. There was also evidence of amyloid formation in vivo: the surfaces of cells expressing wall-bound Als1p, Als5p, Muc1p, or Flo1p were birefringent and bound the fluorescent amyloid-reporting dye thioflavin T. Both of these properties increased upon aggregation of the cells. In addition, amyloid binding dyes strongly inhibited aggregation and flocculation. The results imply that amyloid formation is an intrinsic property of yeast cell adhesion proteins from many gene families and that amyloid formation is an important component of cellular aggregation mediated by these proteins. en_US
dc.language.iso en en_US
dc.title Yeast Cell Adhesion Molecules Have Functional Amyloid-Forming Sequences en_US
dc.type Article en_US
dc.description.version Published en_US
dc.author.school SAS en_US
dc.author.idnumber 200300427 en_US
dc.author.woa N/A en_US
dc.author.department Natural Sciences en_US
dc.description.embargo N/A en_US
dc.relation.journal American Society for MicrobiologyEukaryotic Cell en_US
dc.journal.volume 9 en_US
dc.journal.issue 3 en_US
dc.article.pages 393-404 en_US
dc.identifier.doi http://dx.doi.org/10.1128/EC.00068-09 en_US
dc.identifier.ctation Ramsook, C. B., Tan, C., Garcia, M. C., Fung, R., Soybelman, G., Henry, R., ... & Dranginis, A. M. (2010). Yeast cell adhesion molecules have functional amyloid-forming sequences. Eukaryotic cell, 9(3), 393-404. en_US
dc.author.email roy.khalaf@lau.edu.lb
dc.identifier.url http://ec.asm.org/content/9/3/393.full.pdf+html

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