The T transcription factor functions as a dimer and exhibits a common human polymorphism Gly-177-Asp in the conserved DNA-binding domain

• Published in: FEBS letters Vol. 409; no. 2; pp. 201 - 206
• Main Authors: Papapetrou, C., Edwards, Y.H., Sowden, J.C.
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 09.06.1997
• Subjects: Aspartic Acid - genetics; Conserved Sequence; Dimerization; DNA - metabolism; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - metabolism; Drug Stability; Fetal Proteins - chemistry; Fetal Proteins - metabolism; Glycine - genetics; Humans; Notochord; Polymorphism, Genetic; Protein Binding - genetics; Protein Structure, Tertiary; T dimer; T gene polymorphism; T-Box Domain Proteins; T-box protein; Transcription factor; Transcription Factors - chemistry; Transcription Factors - metabolism; T dimer; T gene polymorphism; Transcription factor; Notochord; T-box protein
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(97)00506-1

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.