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Science 13 October 1995:
Vol. 270. no. 5234, p. 251
DOI: 10.1126/science.270.5234.251
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Perspectives

Brenda J. Andrews, Michael S. Donoviel

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.

The authors are in the Department of Molecular and Medical Genetics, University of Toronto, Toronto M5S 1A8, Canada.




Science. ISSN 0036-8075 (print), 1095-9203 (online)