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Biophys. J. BioFAST: First Published April 22, 2005. doi:10.1529/biophysj.104.057737
© 2005 by the Biophysical Society.

A more recent version of this article appeared on July 1, 2005.
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MUSCLE AND CONTRACTILITY

Hierarchical extensibility in the PEVK domain of skeletal-muscle titin

Attila Nagy 1, László Grama 1, Tamás Huber 2, Pasquale Bianco 1, Károly Trombitás 3, Henk L Granzier 3 and Miklós SZ Kellermayer 1*

1 University of Pécs
2 Universtity of Pécs
3 Washington State University

* To whom correspondence should be addressed. E-mail: miklos.kellermayer.jr{at}aok.pte.hu.

Submitted on January 6, 2005
Revised on March 18, 2005
Accepted on 15 April 2005


  Abstract
Titin is the main determinant of passive muscle force. Physiological extension of titin derives largely from its PEVK (Pro-Glu-Val-Lys) domain which has a different length in different muscle types. Here we characterized the elasticity of the full-length, human soleus PEVK domain by mechanically manipulating its contiguous, recombinant sub-domain segments: an N-terminal (PEVKI), a middle (PEVKII) and a C-terminal one third (PEVKIII). Measurement of the apparent persistence lengths revealed a hierarchical arrangement according to local flexibility: the N-terminal PEVKI is the most rigid and the C-terminal PEVKIII is the most flexible segment within the domain. Immunoelectron microscopy supported the hierarchical extensibility within the PEVK domain. The effective persistence lengths decreased as a function of ionic strength, as predicted by the Odijk-Skolnick-Fixman model of polyelectrolyte chains. The ionic strength dependence of persistence length was similar in all segments, indicating that the residual differences in the elasticity of the segments derives from non-electrostatic mechanisms.

Key Words: immunoelectron microscopy, polyelectrolyte chain, recombinant protein fragments, single-molecule AFM, titin, wormlike chain




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Copyright © 2005 by the Biophysical Society.