Abstract
A highly specific method for the dissociation of protein dimers has been developed. The method involves exposure of the dimers to free leucine at a concentration ranging between 3 and 10 mM. Using this method it has been possible to dissociate goat uterine oestrogen receptor homodimers, heterodimers formed between the non-activated oestrogen receptor (naER) and the oestrogen receptor activation factor (E-RAF) of the goat uterus, c-jun homodimers derived from bovine bone marrow and also glucocorticoid receptor homodimers isolated from rat liver cytosol. The pattern of dimer dissociation by leucine clearly differentiates two classes of proteins. The first is represented by steroid hormone receptors where dimerization is apparently contributed by both coiled-coil dimerization interfaces and the conserved heptad repeats of leucine. The second is represented by oncoproteins like c-fos and c-jun which dimerize through the exclusive involvement of leucine zippers. The patterns of dissociation of these two groups of proteins from the concerned affinity columns are distinctly different. This indicates a possibility that the elution pattern may be used as a yardstick to determine whether two proteins dimerize through the exclusive involvement of leucine zippers or whether coiled-coil interfaces are also involved in the dimerization process.
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