Y. Katankhaykovich et Y. Shaul, RFX1, A SINGLE DNA-BINDING PROTEIN WITH A SPLIT DIMERIZATION DOMAIN, GENERATES ALTERNATIVE COMPLEXES, The Journal of biological chemistry, 273(38), 1998, pp. 24504-24512
The transcription of various viral and cellular genes is regulated by
palindromic and nonpalindromic DNA sites resembling the EP element of
the hepatitis B virus enhancer, which generate similar DNA-protein com
plexes. The upper EP complex contains homodimers of the transcription
regulator RFX1. We show that RFX1 possesses a split, extended dimeriza
tion domain composed of several evolutionarily conserved boxes, one of
which was previously shown to mediate dimerization. Such an unusually
long and complex dimerization domain could potentially serve for gene
rating multiple complexes. In addition to the previously characterized
complex, RFX1 generated a novel DNA-protein complex of extremely low
mobility, formed only with palindromic DNA sites. Different deletions
within the dimerization domain altered the relative abundance of the t
wo complexes, suggesting an interplay between them. Formation of the l
ow mobility complex correlated with transcriptional repression, in tha
t both activities were mediated by several portions of the conserved r
egion. Our results propose a mechanism by which the extended dimerizat
ion domain mediates the formation of alternative homodimeric complexes
, which differ in the nature of the intersubunit interaction. By parti
cipating in different types of interactions, this domain may regulate
the relative abundance of the different complexes, thus affecting tran
scriptional activity.