| Literature DB >> 1577169 |
Abstract
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.Entities:
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Year: 1992 PMID: 1577169 DOI: 10.1016/0014-5793(92)80260-n
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124