Article abstract
Nature Chemical Biology 5, 857 - 862 (2009)
Published online: 20 September 2009 | doi:10.1038/nchembio.220
The yeast Wsc1 cell surface sensor behaves like a nanospring in vivo
Vincent Dupres1,3, David Alsteens1,3, Sabrina Wilk2, Benjamin Hansen2, Jürgen J Heinisch2 & Yves F Dufrêne1
Abstract
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.
- Unité de Chimie des Interfaces, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.
- Universität Osnabrück, Fachbereich Biologie/Chemie, AG Genetik, Osnabrück, Germany.
- These authors contributed equally to this work.
Correspondence to: Yves F Dufrêne1 e-mail: yves.dufrene@uclouvain.be
Correspondence to: Jürgen J Heinisch2 e-mail: juergen.heinisch@biologie.uni-osnabrueck.de
