UV cross-linking identifies four polypeptides that require the TATA box to bind to the Drosophila hsp70 promoter
- Washington Univ., St. Louis, MO (USA)
A protein fraction that requires the TATA sequence to bind to the hsp70 promoter has been partially purified from nuclear extracts of Drosophila embryos. This TATA factor produces a large DNase I footprint that extends from -44 to +35 on the promoter. A mutation that changes TATA to TATG interferes both with the binding of this complex and with the transcription of the hsp70 promoter in vitro, indicating that this interaction is important for transcriptional activity. Using a highly specific protein-DNA cross-linking assay, we have identified four polypeptides that require the TATA sequence to bind to the hsp70 promoter. Polypeptides of 26 and 42 kilodaltons are in intimate contact with the TATA sequence. Polypeptides of 150 and 60 kilodaltons interact within the region from +24 to +47 in a TATA-dependent manner. Both the extended footprint and the polypeptides identified by UV cross-linking indicate that the Drosophila TATA factor is a multicomponent complex.
- OSTI ID:
- 6611543
- Journal Information:
- Molecular and Cellular Biology; (USA), Vol. 10:8; ISSN 0270-7306
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
DNA
BIOASSAY
POLYPEPTIDES
AMINO ACID SEQUENCE
BIOCHEMICAL REACTION KINETICS
CELL NUCLEI
CROSS-LINKING
DNA-ASE
DROSOPHILA
EMBRYOS
FRACTIONATION
MOLECULAR BIOLOGY
MUTATIONS
TRANSCRIPTION
ULTRAVIOLET RADIATION
ANIMALS
ARTHROPODS
CELL CONSTITUENTS
CHEMICAL REACTIONS
DIPTERA
ELECTROMAGNETIC RADIATION
ENZYMES
ESTERASES
FLIES
FRUIT FLIES
HYDROLASES
INSECTS
INVERTEBRATES
KINETICS
MOLECULAR STRUCTURE
NUCLEIC ACIDS
ORGANIC COMPOUNDS
PEPTIDES
PHOSPHODIESTERASES
POLYMERIZATION
PROTEINS
RADIATIONS
REACTION KINETICS
SEPARATION PROCESSES
550201* - Biochemistry- Tracer Techniques