The Drosophila 110-kDa transcription factor TFIID subunit directly interacts with the N-terminal region of the 230-kDa subunit.

AUTOR(ES)

Kokubo, T

RESUMO

Transcription initiation factor TFIID is a multimeric protein complex that plays a central role in transcriptional regulation by facilitating promoter responses to various activators. cDNAs encoding the 110-kDa subunit of Drosophila TFIID (p110) were isolated with a degenerate oligodeoxynucleotide probe based on an amino acid sequence of the purified protein. The entire cDNA sequence contains an open reading frame encoding a 921-amino acid polypeptide with a calculated molecular mass of 99,337 Da. The recombinant protein expressed in Sf9 cells via a baculovirus vector interacts directly with the 230-kDa subunit of TFIID (p230). Together with the previous observation that the TATA box-binding subunit of TFIID (TFIID tau or TBP) interacts directly with only p230 among the TFIID subunits, this result suggests that p110 forms a complex with TFIID tau via p230. A binding study using various p230 mutants indicated that both p110 and TFIID tau interact with the N-terminal 352-amino acid portion of p230, suggesting a functional communication between p110 and TFIID tau via p230 interactions.

Documentos Relacionados

• Interaction between the N-terminal domain of the 230-kDa subunit and the TATA box-binding subunit of TFIID negatively regulates TATA-box binding.
• A region of the 85-kilodalton (kDa) subunit of phosphatidylinositol 3-kinase binds the 110-kDa catalytic subunit in vivo.
• Phytochrome requires the 6-kDa N-terminal domain for full biological activity.
• The Drosophila homologue of the 64 kDa subunit of cleavage stimulation factor interacts with the 77 kDa subunit encoded by the suppressor of forked gene
• The 31-kDa precursor of interleukin 1 alpha is myristoylated on specific lysines within the 16-kDa N-terminal propiece.