Isolation of Xenopus laevis TFIID subunit p22 reveals two distinct structural regions.
A cDNA clone encoding a Xenopus laevis (Xl) homologue of the TATA box-binding factor TFIID subunit p22, which shows similarities to histones H2B and H3, was isolated and sequenced. The deduced 164-amino-acid (aa) sequence was compared to those of homologues cloned from human and Drosophila melanogaster (Dm). Analysis showed that the TFIID subunit p22 consists of an approx. 60-aa less-conserved N-terminus and approx. 100-aa highly-conserved C terminus.
Hasegawa
S
S
Laboratory of Developmental Biology, Department of Cellular Biology, Institute of Molecular and Cellular Biosciences, the University of Tokyo, Japan.
Choi
B I
BI
Horikoshi
M
M
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D004331:Drosophila melanogaster / Q000235:genetics; D006657:Histones / Q000737:chemistry; D006801:Humans; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship; D035362:Transcription Factor TFIID; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics; D014982:Xenopus laevis / Q000235:genetics
D018076:DNA, Complementary; D004268:DNA-Binding Proteins; D006657:Histones; D035362:Transcription Factor TFIID; D014157:Transcription Factors