A 22-amino-acid peptide restores DNA-binding activity to dimerization-defective mutants of the estrogen receptor.
We have identified residues within the estrogen receptor that are required for dimerization and high-affinity DNA binding. A 22-amino-acid peptide encompassing these residues was sufficient to restore DNA-binding activity to a mutant receptor lacking most of the hormone-binding domain. Point mutagenesis of the fusion protein confirmed that this sequence continued to mediate dimerization in a manner similar to that within the native receptor, although its position relative to the DNA-binding domain was appreciably altered.
Lees
J A
JA
Molecular Endocrinology Laboratory, Imperial Cancer Research Fund, London, United Kingdom.
Fawell
S E
SE
White
R
R
Parker
M G
MG
D000595:Amino Acid Sequence; D000818:Animals; D004252:DNA Mutational Analysis; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D066298:In Vitro Techniques; D046911:Macromolecular Substances; D051379:Mice; D008969:Molecular Sequence Data; D010455:Peptides / Q000494:pharmacology*; D011960:Receptors, Estrogen / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D013329:Structure-Activity Relationship; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism*
D004268:DNA-Binding Proteins; D046911:Macromolecular Substances; D010455:Peptides; D011960:Receptors, Estrogen; D011994:Recombinant Proteins; D014157:Transcription Factors