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

Autor:	Jérôme Dehullu, Marion Mathelié-Guinlet, Peter N. Lipke, Felipe Viela, Sviatlana Filimonava, Yves F. Dufrêne, Jason M. Rauceo
Přispěvatelé:	UCL - SST/LIBST - Louvain Institute of Biomolecular Science and Technology
Jazyk:	angličtina
Rok vydání:	2021
Předmět:	0301 basic medicine Mating type Saccharomyces cerevisiae Proteins QH301-705.5 Saccharomyces cerevisiae Medicine (miscellaneous) 02 engineering and technology General Biochemistry Genetics and Molecular Biology Article 03 medical and health sciences Fungal biology Agglutinin Single-molecule biophysics Biology (General) biology Chemistry Force spectroscopy Adhesion 021001 nanoscience & nanotechnology biology.organism_classification Cell aggregation Yeast 030104 developmental biology Mating of yeast Biophysics Stress Mechanical 0210 nano-technology General Agricultural and Biological Sciences Mating Factor
Zdroj:	Communications Biology, Vol 4, Iss 1, Pp 1-8 (2021) Communications Biology, Vol. 4, no.1, p. 33 (2021) Communications Biology
ISSN:	2399-3642
Popis:	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 “α” 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 α-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 H273 of α-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. Mathelié-Guinlet et al. investigate the molecular binding mechanisms of sexual agglutinins in budding yeast Saccharomyces cerevisiae. They report that mechanical tension enhances the strength of agglutinin interactions, supporting a new model in which physical stress induces conformational changes in the binding sites of agglutinins.
Databáze:	OpenAIRE
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