منابع مشابه
Clamping the clamp of RNA polymerase.
Bacterial NusG and its archaeal and eukaryal orthologues Spt5 are the only general transcription factors conserved across the three domains of life. The best studied among them, NusG, is found to be associated with the majority of the transcribed genes in the genome (with its paralogue RfaH picking up the slack) (Belogurov et al, 2009), and is implicated in regulating the lateral mobility of RN...
متن کاملEnhancement of RNA Interference Effect in P19 EC Cells by an RNA-dependent RNA Polymerase
Background: RNA interference (RNAi) is a phenomenon uses double-stranded RNA (dsRNA) to specifically inhibit gene expression. The non-specific silencing caused by interferon response to dsRNA in mammalian cells limits the potential of utilizing RNAi to study gene function. Duplexes of 21-nucleotide short interfering dsRNA (siRNA) inhibit gene expression by RNAi. In some organisms, siRNA can als...
متن کاملThe X-ray crystal structure of the euryarchaeal RNA polymerase in an open clamp configuration
The archaeal transcription apparatus is closely related to the eukaryotic RNA polymerase II (Pol II) system. Archaeal RNA polymerase (RNAP) and Pol II evolved from a common ancestral structure and the euryarchaeal RNAP is the simplest member of the extant archaeal-eukaryotic RNAP family. Here we report the first crystal structure of euryarchaeal RNAP from Thermococcus kodakarensis (Tko). This s...
متن کاملTFE and Spt4/5 open and close the RNA polymerase clamp during the transcription cycle.
Transcription is an intrinsically dynamic process and requires the coordinated interplay of RNA polymerases (RNAPs) with nucleic acids and transcription factors. Classical structural biology techniques have revealed detailed snapshots of a subset of conformational states of the RNAP as they exist in crystals. A detailed view of the conformational space sampled by the RNAP and the molecular mech...
متن کاملHow a DNA polymerase clamp loader opens a sliding clamp.
Processive chromosomal replication relies on sliding DNA clamps, which are loaded onto DNA by pentameric clamp loader complexes belonging to the AAA+ family of adenosine triphosphatases (ATPases). We present structures for the ATP-bound state of the clamp loader complex from bacteriophage T4, bound to an open clamp and primer-template DNA. The clamp loader traps a spiral conformation of the ope...
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ژورنال
عنوان ژورنال: The EMBO Journal
سال: 2011
ISSN: 0261-4189
DOI: 10.1038/emboj.2011.76