A DNA-binding domain of human transcription factor IIIC2.
Transcription factor IIIC2 is required for in vitro transcription of the adenovirus 2 VA1 gene and binds with high affinity to its B-box promoter element which is an 18 bp perfect inverted repeat. Partial proteolysis of TFIIIC2 with chymotrypsin and Staphylococcus aureus V8 protease yielded a species which produced a discrete band in a gel shift assay with about twice the mobility of the undigested complex. Chymotrypsin-digested TFIIIC2 produced a DNase I footprint virtually identical to that of the undigested protein, but the stability of the protein-VA1 DNA complex was drastically reduced and the in vitro transcriptional activity was eliminated. These results indicate that a chymotrypsin-resistant domain of TFIIIC2 binds to the B-box sequence. We speculate that stable binding requires protease sensitive cooperative interactions between TFIIIC2 DNA-binding domains.
Boulanger
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PA
Molecular Biology Institute, University of California, Los Angeles 90024-1570.
L'Etoile
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ND
Berk
A J
AJ
D000260:Adenoviruses, Human / Q000235:genetics*; D002460:Cell Line; D002918:Chymotrypsin; D004279:DNA, Viral / Q000235:genetics* / Q000378:metabolism; D003850:Deoxyribonuclease I; D005814:Genes, Viral; D006801:Humans; D010446:Peptide Fragments / Q000378:metabolism; D011485:Protein Binding; D012367:RNA, Viral / Q000235:genetics; D012697:Serine Endopeptidases; D014157:Transcription Factors / Q000378:metabolism*; D019474:Transcription Factors, TFIII; D014158:Transcription, Genetic; D015678:Viral Structural Proteins / Q000235:genetics*; D000098832:Transcription Factor TFIIIC
D004279:DNA, Viral; D010446:Peptide Fragments; D012367:RNA, Viral; D014157:Transcription Factors; D019474:Transcription Factors, TFIII; D015678:Viral Structural Proteins; D000098832:Transcription Factor TFIIIC; D003850:Deoxyribonuclease I; D012697:Serine Endopeptidases; D002918:Chymotrypsin; C028344:glutamyl endopeptidase