Palindromic assembly of the giant muscle protein titin in the sarcomeric Z-disk

Peijian Zou, Nikos Pinotsis, Stephan Lange, Young-Hwa Song, Alexander Popov, Irene Mavridis, Olga M. Mayans, Mathias Gautel and Matthias Wilmanns ()
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Peijian Zou: EMBL-Hamburg c/o DESY
Nikos Pinotsis: EMBL-Hamburg c/o DESY
Stephan Lange: King's College London
Young-Hwa Song: EMBL-Hamburg c/o DESY
Alexander Popov: EMBL-Hamburg c/o DESY
Irene Mavridis: National Center for Scientific Research ‘Demokritos’
Olga M. Mayans: EMBL-Hamburg c/o DESY
Mathias Gautel: King's College London
Matthias Wilmanns: EMBL-Hamburg c/o DESY

Nature, 2006, vol. 439, issue 7073, 229-233

Abstract: Abstract The Z-disk of striated and cardiac muscle sarcomeres is one of the most densely packed cellular structures in eukaryotic cells1. It provides the architectural framework for assembling and anchoring the largest known muscle filament systems by an extensive network of protein–protein interactions, requiring an extraordinary level of mechanical stability. Here we show, using X-ray crystallography, how the amino terminus of the longest filament component, the giant muscle protein titin, is assembled into an antiparallel (2:1) sandwich complex by the Z-disk ligand telethonin. The pseudosymmetric structure of telethonin mediates a unique palindromic arrangement of two titin filaments, a type of molecular assembly previously found only in protein–DNA complexes. We have confirmed its unique architecture in vivo by protein complementation assays, and in vitro by experiments using fluorescence resonance energy transfer. The model proposed may provide a molecular paradigm of how major sarcomeric filaments are crosslinked, anchored and aligned within complex cytoskeletal networks.

Date: 2006
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DOI: 10.1038/nature04343

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