An RNA Polymerase II Transcription Factor has an Associated DNA-Dependent ATPase (dATPase) Activity Strongly Stimulated by the TATA Region of Promoters

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 86; no. 19; pp. 7356 - 7360
• Main Authors: Conaway, Ronald C., Conaway, Joan Weliky
• Format: Journal Article
• Language: English
• Published: Washington, DC National Academy of Sciences of the United States of America 01.10.1989; National Acad Sciences
• Subjects: Adenosine triphosphatases; Adenosine Triphosphatases - metabolism; Adenoviruses; Animals; Base Sequence; Biochemistry; Biological and medical sciences; Cell Nucleus - enzymology; Chromatography; Chromatography, Affinity; Chromatography, High Pressure Liquid; DNA; DNA Helicases - metabolism; DNA-Binding Proteins; Erythroid-Specific DNA-Binding Factors; Fundamental and applied biological sciences. Psychology; Interleukins; Kinetics; Liver; Liver - enzymology; Male; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Molecular Weight; Oligonucleotide Probes; Promoter regions; Promoter Regions, Genetic; Rats; Rats, Inbred Strains; RNA; Transcription factors; Transcription Factors - isolation & purification; Transcription Factors - metabolism; Transcription, Genetic; Transcription. Transcription factor. Splicing. Rna processing; Vertebrata; Mammalia; Enzymatic activity; Rat; Transcription; ATPase; Rodentia; RNA polymerase 2; Transcription factor; Chromatography
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.86.19.7356

A transcription factor required for synthesis of accurately initiated run-off transcripts by RNA polymerase II has been purified and shown to have an associated DNA-dependent ATPase (dATPase) activity that is strongly stimulated by the TATA region of promoters. This transcription factor, designated δ , was purified more than 3000-fold from extracts of crude rat liver nuclei and has a native molecular mass of approximately 230 kDa. DNA-dependent ATPase (dATPase) and transcription activities copurify when δ is analyzed by hydrophobic interaction and ion-exchange HPLC, arguing that transcription factor δ possesses an ATPase (dATPase) activity. ATPase (dATPase) is specific for adenine nucleotides; ATP and dATP, but not CTP, UTP, or GTP, are hydrolyzed. ATPase (dATPase) is stimulated by both double-stranded and single-stranded DNAs, including pUC18, ssM13, and poly(dT); however, DNA fragments containing the TATA region of either the adenovirus 2 major late or mouse interleukin 3 promoters stimulate ATPase as much as 10-fold more effectively than DNA fragments containing nonpromoter sequences. These data suggest the intriguing possibility that δ plays a critical role in the ATP (dATP)-dependent activation of run-off transcription through a direct interaction with the TATA region of promoters.