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CDNA clone encoding Drosophila transcription factor TFIID.

ABSTRACT: Proper initiation of transcription by RNA polymerase II requires the TATA-consensus-binding transcription factor TFIID. A cDNA clone encoding the Drosophila TFIID protein has been isolated and characterized. The deduced amino acid sequence reveals an open reading frame of 353 residues. The carboxyl-terminal 180 amino acids are approximately 80% identical to yeast TFIID and 88% identical to human TFIID. The amino-terminal portions of the yeast and Drosophila TFIID proteins lack appreciable homology, whereas the Drosophila and human amino termini appear qualitatively similar. In addition, the amino-terminal region of the Drosophila TFIID contains several sequence motifs that are found in other Drosophila proteins which appear to regulate transcription.

SUBMITTER: Muhich ML

PROVIDER: S-EPMC55121 | biostudies-other | 1990 Dec

REPOSITORIES: biostudies-other

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cDNA clone encoding Drosophila transcription factor TFIID.

Muhich M L ML Iida C T CT Horikoshi M M Roeder R G RG Parker C S CS

Proceedings of the National Academy of Sciences of the United States of America 19901201 23

Proper initiation of transcription by RNA polymerase II requires the TATA-consensus-binding transcription factor TFIID. A cDNA clone encoding the Drosophila TFIID protein has been isolated and characterized. The deduced amino acid sequence reveals an open reading frame of 353 residues. The carboxyl-terminal 180 amino acids are approximately 80% identical to yeast TFIID and 88% identical to human TFIID. The amino-terminal portions of the yeast and Drosophila TFIID proteins lack appreciable homolo ...[more]

PMID: 2123550

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