Solution scattering suggests cross-linking function of telethonin in the complex with titin.
Telethonin interacts specifically with the two Z-disk IG-like domains (Z1Z2) at the N terminus of titin, the largest presently known protein. Analytical ultracentrifugation and synchrotron radiation x-ray scattering were employed to study the solution structures of Z1Z2 and its complexes with telethonin, and low resolution models were constructed ab initio from the scattering data. A seven residues-long polyhistidine tag was localized at the tip of the Z1 domain by comparison of independent models of native and His-tagged versions of Z1Z2. The stoichiometry and shape of the complex between the telethonin construct lacking the C terminus and Z1Z2 indicate antiparallel association of two Z1Z2 molecules with telethonin acting as a central linker. The complex of full-length telethonin with Z1Z2 appears to also have a 1:2 stoichiometry at concentrations below 1 mg/ml but dimerizes at higher concentrations. These results suggest a possible role of telethonin in linking titin filaments at the Z-disk periphery.[1]References
- Solution scattering suggests cross-linking function of telethonin in the complex with titin. Zou, P., Gautel, M., Geerlof, A., Wilmanns, M., Koch, M.H., Svergun, D.I. J. Biol. Chem. (2003) [Pubmed]
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