Structural basis for the high activation energy of spectrin self‐association
- 13 February 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 244 (1) , 68-70
- https://doi.org/10.1016/0014-5793(89)81164-0
Abstract
The association of spectrin hetero‐dimer (αβ) to the tetramer (α2β2, which predominates in the cell) is marked by an exceptionally high activation energy, so that the reaction does not proceed measurably in the cold. We have tested the hypothesis that this is due to intra‐dimer association between the α‐ and β‐chain ends, which must be broken before tetramers can form. Two mutant univalent spectrins with association defects at the α and β ends, respectively, and incapable therefore of intra‐dimer bonding, were found to associate rapidly with one another at 4°C. The bimolecular rate constant is greater than for the association of normal dimers by 6 orders of magnitude.Keywords
This publication has 8 references indexed in Scilit:
- Interactions of spectrin in hereditary elliptocytes containing truncated spectrin beta-chains.Journal of Clinical Investigation, 1988
- Analysis of the self-association of human red cell spectrinBiochemistry, 1986
- Mapping the fodrin molecule with monoclonal antibodiesJournal of Molecular Biology, 1983
- Molecular Defect of Spectrin in Hereditary PyropoikilocytosisJournal of Clinical Investigation, 1982
- The molecular structure of human erythrocyte spectrinJournal of Molecular Biology, 1979
- Self‐Association of Human SpectrinEuropean Journal of Biochemistry, 1978
- Structural study of spectrin from human erythrocyte membranesBiochemistry, 1977
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970