Striking homology of the 'variable' N-terminal as well as the 'conserved core' domains of the mouse and human TATA-factors (TFIID).

AUTOR(ES)

Tamura, T

RESUMO

A complementary DNA (cDNA) encoding a mouse TFIID (mIID) was isolated from mouse brain cDNA libraries. The 316 amino acid sequence deduced from cDNA sequences revealed the presence of an amino-terminal region enriched in serine, threonine, and proline (STP-cluster), an uninterrupted stretch of 13 glutamine residues (Q-run), a second STP-cluster, and a conserved carboxy-terminal region. Amino acid sequences of the first STP-cluster and the conserved carboxy-terminal region were identical to those of the human TFIID (hIID). However, the Q-run was considerably shorter than that in hIID and sequences in the second STP-cluster diverged from those of the hIID. The murine TFIID transcript is expressed as a 2 kilobase poly(A)+ RNA in the mouse brain. Southern blot analysis identified a single gene copy per haploid mouse genome.

Documentos Relacionados

• Conserved structural motifs within the N-terminal domain of TFIID tau from Xenopus, mouse and human.
• Mutational analysis of the D1/E1 core helices and the conserved N-terminal region of yeast transcription factor IIB (TFIIB): identification of an N-terminal mutant that stabilizes TATA-binding protein-TFIIB-DNA complexes.
• Requirement for acidic amino acid residues immediately N-terminal to the conserved domain of Saccharomyces cerevisiae TFIID.
• Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains.
• Interaction between the N-terminal domain of the 230-kDa subunit and the TATA box-binding subunit of TFIID negatively regulates TATA-box binding.