Nucleic Acids Research, 1992, Vol. 20, No. 13 3317-3324
© 1992
MOLECULAR BIOLOGY |
Elk-1 protein domains required for direct and SRF-assisted DNA-binding
Institute for Molecular Biology, Hannover Medical School Konstanty-Gutschow-Strasse 8, D-3000 Hannover, Germany
* To whom correspondence should be addressed
Received April 24, 1992. Revised June 1, 1992. Accepted June 1, 1992.
The Ets-related Elk-1 protein can bind to purine-rich DNA target sites in a sequence specific fashion and, in addition, can form a ternary complex with the c-fos serum response element (SRE) and the serum response factor (SRF). We demonstrate that Elk-1 can readily interchange between its different interaction partners. The amino terminal ETS-domain of Elk-1 was shown to be necessary and sufficient for direct ONA-binding activity. For ternary complex formation with the SRE and SRF, both the Elk-1 ETS-domain as well as flanking sequences up to amino acid 169 were required. Removal of sequences between the ETS-domain and amino acids 137–169 did not abolish ternary complex formation. This suggests the Elk-1 region spanning amino acids 137–169 to contain a protein-protein interaction domain. Furthermore, we have shown that a single amino acid exchange introduced into the ETS-domain can drastically alter the direct DNA-binding affinity of Elk-1 without severely affecting SRF-assisted binding to the SRE. Thus, Elk-1 requires different propensities of the ETS-domain to exert its different modes of DNA sequence recognition.
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