Title: | Single-cell fluidic force microscopy reveals stress-dependent molecular interactions in yeast mating |
Author(s): | Mathelie-Guinlet M; Viela F; Dehullu J; Filimonava S; Rauceo JM; Lipke PN; Dufrene YF; |
Address: | "Louvain Institute of Biomolecular Science and Technology, UCLouvain, Croix du Sud, 4-5, bte L7.07.07, 1348, Louvain-la-Neuve, Belgium. Department of Sciences, John Jay College of the City University of New York, New York, NY, 10019, USA. Biology Department, Brooklyn College of the City University of New York, 2900 Bedford Avenue, Brooklyn, NY, 11210, USA. PLipke@brooklyn.cuny.edu. Louvain Institute of Biomolecular Science and Technology, UCLouvain, Croix du Sud, 4-5, bte L7.07.07, 1348, Louvain-la-Neuve, Belgium. yves.dufrene@uclouvain.be" |
DOI: | 10.1038/s42003-020-01498-9 |
ISSN/ISBN: | 2399-3642 (Electronic) 2399-3642 (Linking) |
Abstract: | "Sexual agglutinins of the budding yeast Saccharomyces cerevisiae are proteins mediating cell aggregation during mating. Complementary agglutinins expressed by cells of opposite mating types 'a' and 'alpha' bind together to promote agglutination and facilitate fusion of haploid cells. By means of an innovative single-cell manipulation assay combining fluidic force microscopy with force spectroscopy, we unravel the strength of single specific bonds between a- and alpha-agglutinins (~100 pN) which require pheromone induction. Prolonged cell-cell contact strongly increases adhesion between mating cells, likely resulting from an increased expression of agglutinins. In addition, we highlight the critical role of disulfide bonds of the a-agglutinin and of histidine residue H(273) of alpha-agglutinin. Most interestingly, we find that mechanical tension enhances the interaction strength, pointing to a model where physical stress induces conformational changes in the agglutinins, from a weak-binding folded state, to a strong-binding extended state. Our single-cell technology shows promises for understanding and controlling the complex mechanism of yeast sexuality" |
Keywords: | "Mating Factor/*metabolism Saccharomyces cerevisiae/*metabolism Saccharomyces cerevisiae Proteins/*metabolism Stress, Mechanical;" |
Notes: | "MedlineMathelie-Guinlet, Marion Viela, Felipe Dehullu, Jerome Filimonava, Sviatlana Rauceo, Jason M Lipke, Peter N Dufrene, Yves F eng SC3 GM111133/GM/NIGMS NIH HHS/ Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't England 2021/01/06 Commun Biol. 2021 Jan 4; 4(1):33. doi: 10.1038/s42003-020-01498-9" |