Transcription initiation by RNA polymerase II in vitro. At least two nucleotides must be added to form a stable ternary complex.
نویسندگان
چکیده
منابع مشابه
Architecture of an RNA polymerase II transcription pre-initiation complex.
The protein density and arrangement of subunits of a complete, 32-protein, RNA polymerase II (pol II) transcription pre-initiation complex (PIC) were determined by means of cryogenic electron microscopy and a combination of chemical cross-linking and mass spectrometry. The PIC showed a marked division in two parts, one containing all the general transcription factors (GTFs) and the other pol II...
متن کاملRNA polymerase II at initiation.
R NA polymerase II (RNAPII) is the enzyme responsible for synthesis of all mRNA in higher cells. As the central component of the eukaryotic transcription machinery, RNAPII is the final target of regulatory pathways that are ultimately responsible for cellular development, differentiation, and metabolic control. Publication of the highresolution structure of yeast RNAPII (1, 2) and of a transcri...
متن کاملSnapshots of RNA polymerase II transcription initiation.
Several papers published within the last year utilize innovative techniques for characterizing intermediates in RNA polymerase II transcription. Structural studies of polymerase and its associated factors provide a detailed picture of the transcription machinery, and studies of transcription complex assembly both in vitro and in vivo provide insights into the mechanism of gene expression. A hig...
متن کاملFive intermediate complexes in transcription initiation by RNA polymerase II.
A native gel electrophoresis DNA binding assay was used to resolve complexes formed on the adenovirus Major Late Promoter by general transcription factors and RNA polymerase II. Five sets of complexes containing distinct components were identified. These complexes were generated by sequential binding of TFIID, TFIIA, TFIIB, RNA polymerase II, and TFIIE. The relative positions of each of the fac...
متن کاملRNA polymerase and an activator form discrete subcomplexes in a transcription initiation complex.
Using high-resolution atomic force microscopy (AFM) we show that in a ternary complex of an activator protein, FIS, and RNA polymerase containing the sigma(70) specificity factor at the Escherichia coli tyrT promoter the polymerase and the activator form discrete, but connected, subcomplexes in close proximity. This is the first time that a ternary complex between an activator, a sigma(70) poly...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1987
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)75925-0