DNA-binding and transcriptional properties of human trancription factor TFIID after mild proteolysis
- Texas Univ., Houston, TX (USA). Cancer Center
The existence of separable functions within the human class II general transcription factor TFIID was probed for differential sensitivity to mild proteolytic treatment. Independent of whether TFIID was bound to DNA or free in solution, partial digestion with either one of a variety of nonspecific endoproteases generated a protease-resistant protein product that retained specific DNA recognition, as revealed by DNase I footprinting. However, in contrast to native TFIID, which interacts with the adenovirus major late (ML) promoter over a very broad DNA region, partially proteolyzed TFIID interacted with only a small region of the ML promoter immediately surrounding the TATA sequence. This novel footprint was very similar to that observed with the TATA factor purified from yeast cells. Partially proteolyzed human TFIID could form stable complexes that were resistant to challenge by exogenous templates. It could also nucleate the assembly of transcription complexes on the ML promoter with an efficiency comparable to that of native TFIID, yielding similar levels of transcription initiation. These results suggest a model in which the human TFIID protein is composed of at least two different regions or polypeptides.
- OSTI ID:
- 6370701
- Journal Information:
- Molecular and Cellular Biology; (USA), Vol. 10:7; ISSN 0270-7306
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
DNA
INTERACTIONS
TRANSCRIPTION FACTORS
BIOLOGICAL FUNCTIONS
BIOLOGICAL PATHWAYS
DNA-ASE
GENE RECOMBINATION PROTEINS
GENE REPRESSORS
TRANSCRIPTION
ENZYMES
ESTERASES
FUNCTIONS
HYDROLASES
NUCLEIC ACIDS
NUCLEOPROTEINS
ORGANIC COMPOUNDS
PHOSPHODIESTERASES
PROTEINS
550200* - Biochemistry