Journal ArticleDOI
α-Amanitin: A specific inhibitor of one of two DNA-dependent RNA polymerase activities from calf thymus
Claude Kedinger,Claude Kedinger,M. Gniazdowski,M. Gniazdowski,Jean-Louis Mandel,Jean-Louis Mandel,F. Gissinger,F. Gissinger,Pierre Chambon,Pierre Chambon +9 more
TLDR
α-amanitin selectively inhibits RNA synthesis catalyzed by calf thymus RNA polymerase activity B by interacting with the enzyme and inhibiting chain elongation as discussed by the authors, which can be used to identify the source of RNA synthesis.About:
This article is published in Biochemical and Biophysical Research Communications.The article was published on 1970-01-06. It has received 449 citations till now. The article focuses on the topics: Polymerase & RNA-dependent RNA polymerase.read more
Citations
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Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription.
TL;DR: It is shown that recruitment of the p160 class of coactivators is sufficient for gene activation and for the growth stimulatory actions of estrogen in breast cancer supporting a model in which ER cofactors play unique roles in estrogen signaling.
Journal ArticleDOI
The general transcription machinery and general cofactors.
Mary C. Thomas,Cheng Ming Chiang +1 more
TL;DR: These cofactors are capable of repressing basal transcription when activators are absent and stimulating transcription in the presence of activators, with emphasis on the events occurring after the chromatin has been remodeled but prior to the formation of the first phosphodiester bond.
Journal ArticleDOI
Transcriptional regulation of the ovalbumin and conalbumin genes by steroid hormones in chick oviduct.
G S McKnight,Richard D. Palmiter +1 more
TL;DR: Relative rates of ovalbumin and conalbumin mRNA transcription were measured in isolated oviduct nuclei by allowing endogenous RNA polymerases to synthesize [32P]RNA that was then hybridized to immobilized recombinant DNA containing the respective gene sequences.
Journal ArticleDOI
Specific Inhibition of Nuclear RNA Polymerase II by α-Amanitin
TL;DR: α-Amanitin, a toxic substance from the mushroom Amanita phalloides, is a potent inhibitor of DNA-dependent RNA polymerase II (the nucleoplasmic form) from sea urchin, rat liver, and calf thymus.
Journal ArticleDOI
Site-specific oligonucleotide binding represses transcription of the human c-myc gene in vitro
TL;DR: It is discussed that triplex formation (site-specific RNA binding to a DNA duplex) could serve as the basis for an alternative program of gene control in vivo.
References
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Journal ArticleDOI
Multiple Forms of DNA-dependent RNA Polymerase in Eukaryotic Organisms
TL;DR: Three distinct RNA polymerase activities have been isolated from developing sea urchin embryos, and in rat liver nuclei there are two RNA polymerases activities.
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Studies on the pathogenesis of liver necrosis by α-amanitin. Effect of α-amanitin on ribonucleic acid synthesis and on ribonucleic acid polymerase in mouse liver nuclei
Fiorenzo Stirpe,L. Fiume +1 more
TL;DR: The activity of RNA polymerase activated by Mn(2+) and ammonium sulphate is greatly impaired in liver nuclei isolated from mice poisoned with alpha-amanitin, and is inhibited by the addition of the same toxin in vitro.
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Action of rifamycins on RNA polymerase.
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Isolation and Characterization of a Streptolydigin Resistant RNA Polymerase
TL;DR: It is reported that streptolydigin inhibits chain elongation by E. coli RNA polymerase as was found by Siddhikol et al.4 and that, as is the case of rifampicin resistance1,2, the “core” enzyme (the α2ββ′ structure which itself possesses enzymatic activity) is modified in the resistant mutant.
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The influence of ionic strength and a polyanion on transcription in vitro. I. Stimulation of the aggregate RNA polymerase from rat liver nuclei.
TL;DR: The results indicate that the RNA polymerase is bound to the DNA in the aggregate enzyme as part of an initiation or transcription complex, and the small amount of A-U-rich RNA which is synthesized at 37° is immediately destroyed by degradative enzymes, whereas the G-C-richRNA is much more resistant.