The adenovirus major late transcription factor USF is a member of the helix-loop-helix group of regulatory proteins and binds to DNA as a dimer
| Autor: | P D Gregor, M Sawadogo, Robert G. Roeder |
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| Rok vydání: | 1990 |
| Předmět: |
Transcription
Genetic RNA Splicing Molecular Sequence Data USF2 Biology Molecular cloning Polymerase Chain Reaction DNA-binding protein Upstream Stimulatory Factor chemistry.chemical_compound Biopolymers Leucine Transcription (biology) Complementary DNA Genetics Humans Amino Acid Sequence RNA Messenger Cloning Molecular Base Sequence Basic helix-loop-helix Adenoviruses Human DNA Molecular biology DNA-Binding Proteins chemistry Protein Biosynthesis Upstream Stimulatory Factors Transcription Factors Developmental Biology |
| Zdroj: | Genes & Development. 4:1730-1740 |
| ISSN: | 1549-5477 0890-9369 |
| DOI: | 10.1101/gad.4.10.1730 |
| Popis: | We isolated full-length cDNAs encoding the 43-kD form of human upstream stimulatory factor (USF), a cellular factor required for efficient transcription of the adenovirus major late (AdML) promoter in vitro. Sequence analysis showed USF to be a member of the c-myc-related family of DNA-binding proteins. Using proteins translated in vitro, we identified a DNA-binding domain near the carboxyl terminus, which includes both a helix-loop-helix motif and a leucine repeat. We show that USF interacts with its target DNA as a dimer. The leucine repeat is required for efficient DNA binding of the intact protein and for interactions between full-length and truncated USF proteins. Interestingly, it is not required for DNA binding of the isolated helix-loop-helix domain. The structure of different cDNA clones indicates that USF RNA is differentially spliced, and alternative exon usage may regulate the levels of functional USF protein. |
| Databáze: | OpenAIRE |
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