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Forces in yeast flocculation
- Source :
- Nanoscale. 7:1760-1767
- Publication Year :
- 2015
- Publisher :
- Royal Society of Chemistry (RSC), 2015.
-
Abstract
- In the baker's yeast Saccharomyces cerevisiae, cell-cell adhesion ("flocculation") is conferred by a family of lectin-like proteins known as the flocculin (Flo) proteins. Knowledge of the adhesive and mechanical properties of flocculins is important for understanding the mechanisms of yeast adhesion, and may help controlling yeast behaviour in biotechnology. We use single-molecule and single-cell atomic force microscopy (AFM) to explore the nanoscale forces engaged in yeast flocculation, focusing on the role of Flo1 as a prototype of flocculins. Using AFM tips labelled with mannose, we detect single flocculins on Flo1-expressing cells, showing they are widely exposed on the cell surface. When subjected to force, individual Flo1 proteins display two distinct force responses, i.e. weak lectin binding forces and strong unfolding forces reflecting the force-induced extension of hydrophobic tandem repeats. We demonstrate that cell-cell adhesion bonds also involve multiple weak lectin interactions together with strong unfolding forces, both associated with Flo1 molecules. Single-molecule and single-cell data correlate with microscale cell adhesion behaviour, suggesting strongly that Flo1 mechanics is critical for yeast flocculation. These results favour a model in which not only weak lectin-sugar interactions are involved in yeast flocculation but also strong hydrophobic interactions resulting from protein unfolding.
- Subjects :
- Flocculation
Saccharomyces cerevisiae Proteins
biology
Saccharomyces cerevisiae
Plasma protein binding
Adhesion
Microscopy, Atomic Force
biology.organism_classification
Article
Yeast
Hydrophobic effect
Mannose-Binding Lectins
Biochemistry
Lectins
Yeast flocculation
Cell Adhesion
Biophysics
General Materials Science
Cell adhesion
Hydrophobic and Hydrophilic Interactions
Mannose
Protein Binding
Protein Unfolding
Subjects
Details
- ISSN :
- 20403372 and 20403364
- Volume :
- 7
- Database :
- OpenAIRE
- Journal :
- Nanoscale
- Accession number :
- edsair.doi.dedup.....afba06bd5405099f271aa99de20c10b3