Two different cDNAs encoding TFIID proteins of maize.
Two different complementary DNAs (cDNAs) encoding maize TFIID proteins were isolated from a maize leaf cDNA. Both cDNA sequences reveal two types of TFIID, each encoding an open reading frame of 200 amino acids. The two cDNAs are 76% identical at the DNA level and their putative amino acid sequences differ at only three amino acids. Like TATA box binding proteins from other organisms they show a bipartite structure containing a specific N-terminal region and a highly conserved C-terminal domain expected to be necessary and sufficient for the essential TFIID functions in transcriptional initiation.
Haass
M M
MM
Institut für Biologie III, Albert-Ludwigs-Universität, Freiburg, Germany.
Feix
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D000595:Amino Acid Sequence; D001483:Base Sequence; D015139:Blotting, Southern; D004247:DNA / Q000235:genetics*; D008969:Molecular Sequence Data; D015183:Restriction Mapping; D035362:Transcription Factor TFIID; D014157:Transcription Factors / Q000235:genetics*; D003313:Zea mays / Q000378:metabolism*
D035362:Transcription Factor TFIID; D014157:Transcription Factors; D004247:DNA