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The N-terminal domain of the Flo1 flocculation protein from Saccharomyces cerevisiae binds specifically to mannose Carbohydrates

(2011) EUKARYOTIC CELL. 10(1). p.110-117
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Abstract
Saccharomyces cerevisiae cells possess a remarkable capacity to adhere to other yeast cells, which is called flocculation. Flocculation is defined as the phenomenon wherein yeast cells adhere in clumps and sediment rapidly from the medium in which they are suspended. These cell-cell interactions are mediated by a class of specific cell wall proteins, called flocculins, that stick out of the cell walls of flocculent cells. The N-terminal part of the three-domain protein is responsible for carbohydrate binding. We studied the N-terminal domain of the Flo1 protein (N-Flo1p), which is the most important flocculin responsible for flocculation of yeast cells. It was shown that this domain is both O and N glycosylated and is structurally composed mainly of beta-sheets. The binding of N-Flo1p to D-mannose, alpha-methyl-D-mannoside, various dimannoses, and mannan confirmed that the N-terminal domain of Flo1p is indeed responsible for the sugar-binding activity of the protein. Moreover, fluorescence spectroscopy data suggest that N-Flo1p contains two mannose carbohydrate binding sites with different affinities. The carbohydrate dissociation constants show that the affinity of N-Flo1p for mono-and dimannoses is in the millimolar range for the binding site with low affinity and in the micromolar range for the binding site with high affinity. The high-affinity binding site has a higher affinity for low-molecular-weight (low-MW) mannose carbohydrates and no affinity for mannan. However, mannan as well as low-MW mannose carbohydrates can bind to the low-affinity binding site. These results extend the cellular flocculation model on the molecular level.
Keywords
BREWERS-YEAST, SURFACE, SECONDARY STRUCTURE, GENE FAMILY, CELL-WALL PROTEINS, YEAST FLOCCULATION, CIRCULAR-DICHROISM SPECTRA, IDENTIFICATION, ADHESION, LOCALIZATION

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Chicago
Goossens, Katty VY, Catherine Stassen, Ingeborg Stals, Dagmara S Donohue, Bart Devreese, Henri De Greve, and Ronnie G Willaert. 2011. “The N-terminal Domain of the Flo1 Flocculation Protein from Saccharomyces Cerevisiae Binds Specifically to Mannose Carbohydrates.” Eukaryotic Cell 10 (1): 110–117.
APA
Goossens, K. V., Stassen, C., Stals, I., Donohue, D. S., Devreese, B., De Greve, H., & Willaert, R. G. (2011). The N-terminal domain of the Flo1 flocculation protein from Saccharomyces cerevisiae binds specifically to mannose Carbohydrates. EUKARYOTIC CELL, 10(1), 110–117.
Vancouver
1.
Goossens KV, Stassen C, Stals I, Donohue DS, Devreese B, De Greve H, et al. The N-terminal domain of the Flo1 flocculation protein from Saccharomyces cerevisiae binds specifically to mannose Carbohydrates. EUKARYOTIC CELL. 2011;10(1):110–7.
MLA
Goossens, Katty VY, Catherine Stassen, Ingeborg Stals, et al. “The N-terminal Domain of the Flo1 Flocculation Protein from Saccharomyces Cerevisiae Binds Specifically to Mannose Carbohydrates.” EUKARYOTIC CELL 10.1 (2011): 110–117. Print.
@article{1231797,
  abstract     = {Saccharomyces cerevisiae cells possess a remarkable capacity to adhere to other yeast cells, which is called flocculation. Flocculation is defined as the phenomenon wherein yeast cells adhere in clumps and sediment rapidly from the medium in which they are suspended. These cell-cell interactions are mediated by a class of specific cell wall proteins, called flocculins, that stick out of the cell walls of flocculent cells. The N-terminal part of the three-domain protein is responsible for carbohydrate binding. We studied the N-terminal domain of the Flo1 protein (N-Flo1p), which is the most important flocculin responsible for flocculation of yeast cells. It was shown that this domain is both O and N glycosylated and is structurally composed mainly of beta-sheets. The binding of N-Flo1p to D-mannose, alpha-methyl-D-mannoside, various dimannoses, and mannan confirmed that the N-terminal domain of Flo1p is indeed responsible for the sugar-binding activity of the protein. Moreover, fluorescence spectroscopy data suggest that N-Flo1p contains two mannose carbohydrate binding sites with different affinities. The carbohydrate dissociation constants show that the affinity of N-Flo1p for mono-and dimannoses is in the millimolar range for the binding site with low affinity and in the micromolar range for the binding site with high affinity. The high-affinity binding site has a higher affinity for low-molecular-weight (low-MW) mannose carbohydrates and no affinity for mannan. However, mannan as well as low-MW mannose carbohydrates can bind to the low-affinity binding site. These results extend the cellular flocculation model on the molecular level.},
  author       = {Goossens, Katty VY and Stassen, Catherine and Stals, Ingeborg and Donohue, Dagmara S and Devreese, Bart and De Greve, Henri and Willaert, Ronnie G},
  issn         = {1535-9778},
  journal      = {EUKARYOTIC CELL},
  keyword      = {BREWERS-YEAST,SURFACE,SECONDARY STRUCTURE,GENE FAMILY,CELL-WALL PROTEINS,YEAST FLOCCULATION,CIRCULAR-DICHROISM SPECTRA,IDENTIFICATION,ADHESION,LOCALIZATION},
  language     = {eng},
  number       = {1},
  pages        = {110--117},
  title        = {The N-terminal domain of the Flo1 flocculation protein from Saccharomyces cerevisiae binds specifically to mannose Carbohydrates},
  url          = {http://dx.doi.org/10.1128/EC.00185-10},
  volume       = {10},
  year         = {2011},
}

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