A DNA-binding domain of human transcription factor IIIC2.
AUTOR(ES)
Boulanger, P A
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=334883Documentos Relacionados
- Determinants of DNA-binding specificity of ETS-domain transcription factors.
- DNA-binding specificities of the GATA transcription factor family.
- DNA-binding and transcriptional properties of human transcription factor TFIID after mild proteolysis.
- Sequences flanking the core DNA-binding domain of bovine papillomavirus type 1 E2 contribute to DNA-binding function.
- TUF, the yeast DNA-binding factor specific for UASrpg upstream activating sequences: identification of the protein and its DNA-binding domain.