Yeast Cell Adhesion Molecules Have Functional Amyloid-Forming Sequences
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-a...
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2010
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| Online Access: | http://hdl.handle.net/10725/3369 http://dx.doi.org/10.1128/EC.00068-09 http://ec.asm.org/content/9/3/393.full.pdf+html |
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| _version_ | 1864513461025767424 |
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| author | Khalaf, Roy A. |
| author2 | Ramsook, Caleen B. Tan, Cho Garcia, Melissa C. Fung, Raymond Soybelman, Gregory |
| author2_role | author author author author author |
| author_facet | Khalaf, Roy A. Ramsook, Caleen B. Tan, Cho Garcia, Melissa C. Fung, Raymond Soybelman, Gregory |
| author_role | author |
| dc.creator.none.fl_str_mv | Khalaf, Roy A. Ramsook, Caleen B. Tan, Cho Garcia, Melissa C. Fung, Raymond Soybelman, Gregory |
| dc.date.none.fl_str_mv | 2010 2016-03-21T08:37:47Z 2016-03-21T08:37:47Z 2016-03-21 |
| dc.identifier.none.fl_str_mv | 1535-9778 http://hdl.handle.net/10725/3369 http://dx.doi.org/10.1128/EC.00068-09 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. http://ec.asm.org/content/9/3/393.full.pdf+html |
| dc.language.none.fl_str_mv | en |
| dc.relation.none.fl_str_mv | American Society for MicrobiologyEukaryotic Cell |
| dc.rights.*.fl_str_mv | info:eu-repo/semantics/openAccess |
| dc.title.none.fl_str_mv | Yeast Cell Adhesion Molecules Have Functional Amyloid-Forming Sequences |
| dc.type.none.fl_str_mv | Article info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/article |
| description | 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. |
| eu_rights_str_mv | openAccess |
| format | article |
| id | LAURepo_e7ca26cfa682dd9abeb425134150bf59 |
| identifier_str_mv | 1535-9778 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. |
| language_invalid_str_mv | en |
| network_acronym_str | LAURepo |
| network_name_str | Lebanese American University repository |
| oai_identifier_str | oai:laur.lau.edu.lb:10725/3369 |
| publishDate | 2010 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| spelling | Yeast Cell Adhesion Molecules Have Functional Amyloid-Forming SequencesKhalaf, Roy A.Ramsook, Caleen B.Tan, ChoGarcia, Melissa C.Fung, RaymondSoybelman, GregoryThe 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.PublishedN/A2016-03-21T08:37:47Z2016-03-21T08:37:47Z20102016-03-21Articleinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article1535-9778http://hdl.handle.net/10725/3369http://dx.doi.org/10.1128/EC.00068-09Ramsook, 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.http://ec.asm.org/content/9/3/393.full.pdf+htmlenAmerican Society for MicrobiologyEukaryotic Cellinfo:eu-repo/semantics/openAccessoai:laur.lau.edu.lb:10725/33692016-08-17T08:58:01Z |
| spellingShingle | Yeast Cell Adhesion Molecules Have Functional Amyloid-Forming Sequences Khalaf, Roy A. |
| status_str | publishedVersion |
| title | Yeast Cell Adhesion Molecules Have Functional Amyloid-Forming Sequences |
| title_full | Yeast Cell Adhesion Molecules Have Functional Amyloid-Forming Sequences |
| title_fullStr | Yeast Cell Adhesion Molecules Have Functional Amyloid-Forming Sequences |
| title_full_unstemmed | Yeast Cell Adhesion Molecules Have Functional Amyloid-Forming Sequences |
| title_short | Yeast Cell Adhesion Molecules Have Functional Amyloid-Forming Sequences |
| title_sort | Yeast Cell Adhesion Molecules Have Functional Amyloid-Forming Sequences |
| url | http://hdl.handle.net/10725/3369 http://dx.doi.org/10.1128/EC.00068-09 http://ec.asm.org/content/9/3/393.full.pdf+html |