The yeast Wsc1 cell surface sensor behaves like a nanospring in vivo

Autor(en): Dupres, Vincent
Alsteens, David
Wilk, Sabrina
Hansen, Benjamin
Heinisch, Juergen J.
Dufrene, Yves F.
Stichwörter: ATOMIC-FORCE MICROSCOPY; Biochemistry & Molecular Biology; DOMAINS; INTEGRITY; MID2; PATHWAYS; PROTEIN; RECEPTOR; SACCHAROMYCES-CEREVISIAE; SINGLE-MOLECULAR RECOGNITION; SPECTROSCOPY
Erscheinungsdatum: 2009
Herausgeber: NATURE PUBLISHING GROUP
Journal: NATURE CHEMICAL BIOLOGY
Volumen: 5
Ausgabe: 11
Startseite: 857
Seitenende: 862
Zusammenfassung: 
Here we report on in vivo measurement of the mechanical behavior of a cell surface sensor using single-molecule atomic force microscopy. We focus on the yeast wall stress component sensor Wsc1, a plasma membrane protein that is thought to function as a rigid probe of the cell wall status. We first map the distribution of individual histidine-tagged sensors on living yeast cells by scanning the cell surface with atomic force microscopy tips carrying nitrilotriacetate groups. We then show that Wsc1 behaves like a linear nanospring that is capable of resisting high mechanical force and of responding to cell surface stress. Both a genomic pmt4 deletion and the insertion of a stretch of glycines in Wsc1 result in substantial alterations in protein spring properties, supporting the important role of glycosylation at the extracellular serine/threonine-rich region.
ISSN: 15524450
DOI: 10.1038/nchembio.220

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