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</script>The archaeal RNA polymerase (RNAP) shares structural similarities with eukaryotic RNAP II but requires a reduced subset of general transcription factors for promoter-dependent initiation. To deepen our knowledge of cellular transcription, we have determined the structure of the 13-subunit DNA-directed RNAP from Sulfolobus shibatae at 3.35 Å resolution. The structure contains the full complement of subunits, including RpoG/Rpb8 and the equivalent of the clamp-head and jaw domains of the eukaryotic Rpb1. Furthermore, we have identified subunit Rpo13, an RNAP component in the order Sulfolobales, which contains a helix-turn-helix motif that interacts with the RpoH/Rpb5 and RpoA'/Rpb1 subunits. Its location and topology suggest a role in the formation of the transcription bubble.
Models, Molecular, Transcription, Genetic, QH301-705.5, Archaeal Proteins, Molecular Sequence Data, DNA-Directed RNA Polymerases, RNA, Archaeal, Crystallography, X-Ray, Biochemistry, Sulfolobus, Evolution, Molecular, Protein Subunits, Pathology, Amino Acid Sequence, Biology (General), Genetics (life sciences), Biology, Research Article
Models, Molecular, Transcription, Genetic, QH301-705.5, Archaeal Proteins, Molecular Sequence Data, DNA-Directed RNA Polymerases, RNA, Archaeal, Crystallography, X-Ray, Biochemistry, Sulfolobus, Evolution, Molecular, Protein Subunits, Pathology, Amino Acid Sequence, Biology (General), Genetics (life sciences), Biology, Research Article
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| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 1% |
