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

被引:112
作者
Dupres, Vincent [1 ]
Alsteens, David [1 ]
Wilk, Sabrina [2 ]
Hansen, Benjamin [2 ]
Heinisch, Juergen J. [2 ]
Dufrene, Yves F. [1 ]
机构
[1] Catholic Univ Louvain, Unite Chim Interfaces, B-3000 Louvain, Belgium
[2] Univ Osnabruck, Fachbereich Biol Chem, AG Genet, D-4500 Osnabruck, Germany
关键词
ATOMIC-FORCE MICROSCOPY; SINGLE-MOLECULAR RECOGNITION; SACCHAROMYCES-CEREVISIAE; INTEGRITY; PROTEIN; RECEPTOR; DOMAINS; MID2; SPECTROSCOPY; PATHWAYS;
D O I
10.1038/nchembio.220
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:857 / 862
页数:6
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