4.7 Article

Single-cell fluidic force microscopy reveals stress-dependent molecular interactions in yeast mating

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COMMUNICATIONS BIOLOGY
卷 4, 期 1, 页码 -

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NATURE RESEARCH
DOI: 10.1038/s42003-020-01498-9

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资金

  1. European Research Council (ERC) under the European Union's Horizon 2020 research and innovation program [693630]
  2. FNRS-WELBIO [WELBIO-CR-2015A-05]
  3. National Fund for Scientific Research (FNRS)
  4. Research Department of the Communaute francaise de Belgique (Concerted Research Action)
  5. US National Institute of General Medical Sciences [SC3GM111133]

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This study investigates the strength of bonds between a- and alpha-agglutinins in budding yeast during mating, revealing insights into the complex mechanism of cell aggregation. Prolonged cell-cell contact and mechanical tension were found to enhance adhesion between mating cells, pointing to potential conformational changes in agglutinins under physical stress.
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 (similar to 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.

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