Self-association of spectrin's repeating segments

Biochemistry
G B RalstonD Branton

Abstract

We have examined the self-association behavior in solution of one of the repeating conformational segments of Drosophila spectrin, D-alpha-14, as well as of the two-segment unit, D-alpha-14,15. In both polypeptides, sedimentation equilibrium and nondenaturing gel electrophoresis detect a reversible, moderate affinity (K2 approximately equal to 10(4) M-1) dimerization reaction. Equilibration between monomer and dimer is kinetically limited near 5 degrees C, but occurs at a measurable rate at temperatures > or = 20 degrees C. The temperature dependence for equilibration is consistent with the requirement for extensive disruption of helix-helix packing as the reaction proceeds in either direction. Hydrodynamic studies by means of sedimentation velocity confirm that in solution the C helix in the monomer of D-alpha_14 is folded back to interact with the A and B helices, and that the form of monomeric subunit observed in the crystal structure, in which the A and B helices are continuous, does not persist in the monomer in solution. Both the dimer of D-alpha-14 and the monomer of D-alpha-14,15 appear to be twice the length of the D-alpha-14 monomer, while the frictional ration of the D-alpha-14,15 dimer is consistent with four end-to...Continue Reading

References

Aug 1, 1978·European Journal of Biochemistry·E Ungewickell, W Gratzer
Mar 28, 1977·Biochimica Et Biophysica Acta·G RalstonM White
Aug 1, 1994·Biophysical Journal·J Garcia de la TorreJ J Lopez Cascales

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Citations

Feb 1, 1997·Current Opinion in Biotechnology·W F Stafford
Jul 30, 1999·Biochemical and Biophysical Research Communications·J P NewtonD J Harvey

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