Amanitin-resistant RNA polymerase II mutations are in the enzyme's largest subunit.
نویسندگان
چکیده
منابع مشابه
Giardia lamblia RNA polymerase II: amanitin-resistant transcription.
Giardia lamblia is an early branching eukaryote, and although distinctly eukaryotic in its cell and molecular biology, transcription and translation in G. lamblia demonstrate important differences from these processes in higher eukaryotes. The cyclic octapeptide amanitin is a relatively selective inhibitor of eukaryotic RNA polymerase II (RNAP II) and is commonly used to study RNAP II transcrip...
متن کاملAlpha-amanitin blocks translocation by human RNA polymerase II.
Our laboratory has developed methods for transient state kinetic analysis of human RNA polymerase II elongation. In these studies, multiple conformations of the RNA polymerase II elongation complex were revealed by their distinct elongation potential and differing dependence on nucleoside triphosphate substrate. Among these are conformations that appear to correspond to different translocation ...
متن کاملA unique structure at the carboxyl terminus of the largest subunit of eukaryotic RNA polymerase II.
Purified eukaryotic nuclear RNA polymerase II consists of three subspecies that differ in the apparent molecular masses of their largest subunit, designated IIo, IIa, and IIb for polymerase species IIO, IIA, and IIB, respectively. Subunits IIo, IIa, and IIb are the products of a single gene. We present here the amino acid composition of calf thymus subunits IIa and IIb and the C-terminal amino ...
متن کاملAffinity isolation of RNA polymerase II on amanitin-Sepharose.
We report here the first case of an affinity isolation of eukaryotic RNA polymerase II. The procedure employs an affinity matrix composed of alpha-amanitin coupled to Sepharose 4B via a ten atom spacer. RNA polymerase II from either calf thymus or wheat germ binds to the amanitin-Sepharose, as indicated by subsequent elution with sodium dodecylsulfate-containing buffer and analysis by polyacryl...
متن کاملA protein kinase from wheat germ that phosphorylates the largest subunit of RNA polymerase II.
A protein kinase from wheat germ that phosphorylates the largest subunit of RNA polymerase IIA has been partially purified and characterized. The kinase has a native molecular weight of about 200 kilodaltons. This kinase utilizes Mg2+ and ATP and transfers about 20 phosphates to the heptapeptide repeats Pro-Thr-Ser-Pro-Ser-Tyr-Ser in the carboxyl-terminal domain of the 220-kilodalton subunit of...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1983
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)43925-1