The T transcription factor functions as a dimer and exhibits a common human polymorphism Gly-177-Asp in the conserved DNA-binding domain.
T is a transcription factor which activates transcription by binding to repeated arrangements of the dodecamer 5'-AGGTGTGAAATT-3'. Using in vitro synthesised T protein, we have demonstrated that T binds to its target DNA as a homodimer and that truncated protein containing only the N-terminal 233 amino-acid residues, which comprise the DNA-binding domain, can form a dimer. We also report a common human polymorphism, Gly-177-Asp, within the DNA-binding domain at a position which is a conserved glycine residue in T homologues from other vertebrates. The proposition that T forms heterodimers with other members of the T-box transcription factor family and the implications for disorders of axial development are discussed.
Papapetrou
C
C
MRC Human Biochemical Genetics Unit, University College London, UK.
Edwards
Y H
YH
Sowden
J C
JC
D001224:Aspartic Acid / Q000235:genetics*; D017124:Conserved Sequence; D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D019281:Dimerization; D004355:Drug Stability; D005326:Fetal Proteins / Q000737:chemistry* / Q000378:metabolism*; D005998:Glycine / Q000235:genetics*; D006801:Humans; D011110:Polymorphism, Genetic; D011485:Protein Binding / Q000235:genetics; D017434:Protein Structure, Tertiary; D020825:T-Box Domain Proteins; D014157:Transcription Factors / Q000737:chemistry* / Q000378:metabolism; D000098908:Brachyury Protein
D001224:Aspartic Acid; D004247:DNA; D004268:DNA-Binding Proteins; D005326:Fetal Proteins; D005998:Glycine; D020825:T-Box Domain Proteins; D014157:Transcription Factors; D000098908:Brachyury Protein