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The titin Y9P variant of the titin I27 module: structural determinants of its revisited nanomechanics

AutorOroz, J.; Bruix, M. ; Laurents, D.V. ; Galera-Prat, Albert ; Schönfelder, J.; Cañada, F. Javier ; Carrión-Vázquez, Mariano Sixto
Fecha de publicación2016
EditorCell Press
CitaciónStructure 24: 606- 616 (2016)
ResumenThe I27 module from human cardiac titin has become a standard in protein nanomechanics. A proline-scanning study of its ¿mechanical clamp¿ found three mechanically hypomorphic mutants and a paradoxically hypermorphic one (Y9P). Both types of mutants have been commonly used as substrates of several protein unfoldase machineries in studies relating protein mechanostability to translocation or degradation rates. Using AFM-based single-molecule force spectroscopy, polyprotein engineering and steered molecular dynamics simulations we show that, unexpectedly, the mechanostability of the Y9P variant is comparable to the wild type. Furthermore, the NMR analysis of homomeric polyproteins of this variant suggests that these constructs may induce slight structural perturbations in the monomer, and enables us to explain some minor differences in this variant¿s properties; namely the abolishment of the mechanical unfolding intermediate and a reduced thermal stability. Our results clarify a previously reported paradoxical result in protein nanomechanics and contribute to refine our toolbox for understanding the unfolding mechanism used by translocases and degradation machines.
URIhttp://hdl.handle.net/10261/162185
Identificadoresdoi: 10.1016/j.str.2016.02.016
issn: 0969-2126
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