ArticleThe Journal of biological chemistry2010
Deletion of switch 3 results in an archaeal RNA polymerase that is defective in transcript elongation.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Article
- FttA is a CPSF73 homologue that terminates transcription in Archaea.Nature microbiology · 2020Article
- The cutting edge of archaeal transcription.Emerging topics in life sciences · 2018Article
- Archaeal RNA polymerase arrests transcription at DNA lesions.Transcription · 2017Article
- An archaeal histone is required for transformation of Thermococcus kodakarensis.Journal of bacteriology · 2012Article
- A dual switch controls bacterial enhancer-dependent transcription.Nucleic acids research · 2012Article
- Overview of the genetic tools in the Archaea.Frontiers in microbiology · 2012Article
- Genetics Techniques for Thermococcus kodakarensis.Frontiers in microbiology · 2012Article
- Genetic tool development underpins recent advances in thermophilic whole-cell biocatalysts.Microbial biotechnology · 2011Review
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2 authors.
Funding
Abstract
Switch 3 is a polypeptide loop conserved in all multisubunit DNA-dependent RNA polymerases (RNAPs) that extends into the main cleft of the RNAP and contacts each base in a nascent transcript as that base is released from the internal DNA-RNA hybrid. Plasmids have been constructed and transformed into Thermococcus kodakaraensis, which direct the constitutive synthesis of the archaeal RNAP subunit RpoB with an N-terminal His(6) tag and the Switch 3 loop either intact (wild-type) or deleted (DeltaS3). RNAPs containing these plasmid-encoded RpoB subunits were purified, and, in vitro, the absence of Switch 3 had no negative effects on transcription initiation or elongation complex stability but reduced the rate of transcript elongation. The defect in elongation occurred at every template position and increased the sensitivity of the archaeal RNAP to intrinsic termination. Comparing these properties and those reported for a bacterial RNAP lacking Switch 3 argues that this loop functions differently in the RNAPs from the two prokaryotic domains. The close structural homology of archaeal and eukaryotic RNAPs would predict that eukaryotic Switch 3 loops likely conform to the archaeal rather than bacterial functional paradigm.
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