Sequential Unfolding of Beta Helical Protein by Single-Molecule Atomic Force Microscopy

Abstract : The parallel βhelix is a common fold among extracellular proteins, however its mechanical properties remain unexplored. In Gram-negative bacteria, extracellular proteins of diverse functions of the large 'TpsA' family all fold into long βhelices. Here, single-molecule atomic force microscopy and steered molecular dynamics simulations were combined to investigate the mechanical properties of a prototypic TpsA protein, FHA, the major adhesin of Bordetella pertussis. Strong extension forces were required to fully unfold this highly repetitive protein, and unfolding occurred along a stepwise, hierarchical process. Our analyses showed that the extremities of the βhelix unfold early, while central regions of the helix are more resistant to mechanical unfolding. In particular, a mechanically resistant subdomain conserved among TpsA proteins and critical for secretion was identified. This nucleus harbors structural elements packed against the βhelix that might contribute to stabilizing the N-terminal region of FHA. Hierarchical unfolding of the βhelix in response to a mechanical stress may maintain β-helical portions that can serve as templates for regaining the native structure after stress. The mechanical properties uncovered here might apply to many proteins with β-helical or related folds, both in prokaryotes and in eukaryotes, and play key roles in their structural integrity and functions.
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PLoS ONE, Public Library of Science, 2013, 8 (8), pp.e73572. 〈10.1371/journal.pone.0073572〉
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Soumis le : lundi 18 décembre 2017 - 10:00:01
Dernière modification le : mardi 3 juillet 2018 - 11:23:05

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David Alsteens, Nicolas Martinez, Marc Jamin, Françoise Jacob-Dubuisson, Daniel J. Müller. Sequential Unfolding of Beta Helical Protein by Single-Molecule Atomic Force Microscopy. PLoS ONE, Public Library of Science, 2013, 8 (8), pp.e73572. 〈10.1371/journal.pone.0073572〉. 〈hal-01666101〉

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