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.
Mesh Terms:
Cloning, Molecular, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Humans, Models, Molecular, Models, Statistical, Muscle Proteins, Muscles, Mutagenesis, Site-Directed, Protein Binding, Protein Kinases, Protein Structure, Tertiary, Scattering, Radiation, Statistics as Topic, Synchrotrons, Two-Hybrid System Techniques, Ultracentrifugation, X-Rays
J. Biol. Chem.
Date: Jan. 24, 2003
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