A Heterodimeric Transcriptional Repressor Becomes Crystal Clear

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Science  13 Oct 1995:
Vol. 270, Issue 5234, pp. 251
DOI: 10.1126/science.270.5234.251


The crystal structure of a heterodimeric transcriptional repressor from yeast, a1/alpha-2, reported in the same issue of Science, reveals a mechanism for ensuring DNA-binding specificity that may be used by many other DNA-binding heterodimers. B. J. Andrews and M. S. Donoviel explain how sequence specificity is controlled by the spacing between the proteins, which must match that of the contact points on the DNA. The carboxyl-terminal tail of alpha-2 is the key interface with a1 and determines the interprotein distance.