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Literature summary extracted from

  • Hou, L.; Klug, G.; Evguenieva-Hackenberg, E.
    Archaeal DnaG contains a conserved N-terminal RNA-binding domain and enables tailing of rRNA by the exosome (2014), Nucleic Acids Res., 42, 12691-12706.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.101 gene dnaG, sequence comparisons, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli, coexpression with His6-tagged Rrp4, Csl4, Rrp41 and Rrp42, and Strep-tagged Csl4 Saccharolobus solfataricus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.101 E175Q site-directed mutagenesis of the TOPRIM domain, DnaGE175Q has a poly(rA) preference like wild-type DnaG Saccharolobus solfataricus
2.7.7.101 K6A/Y7A site-directed mutagenesis of the N-terminal domain Saccharolobus solfataricus
2.7.7.101 additional information a fusion protein consisting of the full-length Csl4 and the N-terminal domain of enzyme DnaG catalyzes the degradation of A-rich RNA by the exosome. Construction of a His-tagged enzyme mutant lacking the N-terminal domain, analysis of interaction between the Csl4 exosome and His6-DnaG-DELTANT Saccharolobus solfataricus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.101 Mg2+ required Saccharolobus solfataricus

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.101 Saccharolobus solfataricus P95980 gene dnaG
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.101 recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli, copurification of the His6-tagged wild-type enzyme with His6-tagged Rrp4, Csl4, Rrp41 and Rrp42, and Strep-tagged Csl4 Saccharolobus solfataricus

Subunits

EC Number Subunits Comment Organism
2.7.7.101 More archaeal DnaG contains N- and C-terminal domains flanking a TOPRIM domain. The N-terminal domain is a RNA-binding domain with poly(rA)-preference cooperating with the TOPRIM domain in binding of RNA Saccharolobus solfataricus

Synonyms

EC Number Synonyms Comment Organism
2.7.7.101 DnaG
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.101 37
-
 assay at Saccharolobus solfataricus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.101 7.9
-
 assay at Saccharolobus solfataricus

General Information

EC Number General Information Comment Organism
2.7.7.101 evolution phylogenetic analysis of DnaG proteins in archaea, overview Saccharolobus solfataricus
2.7.7.101 additional information comparison of bacterial and archaeal DnaG and composition of reconstituted Sulfolobus solfataricus exosomes, overview Saccharolobus solfataricus
2.7.7.101 physiological function enzyme DnaG strongly binds native and in vitro transcribed rRNA and enables its polynucleotidylation by the exosome. The N-terminal domain of DnaG is a RNA-binding domain with poly(rA)-preference cooperating with the TOPRIM domain in binding of RNA. The C-terminal domain, but not the N-terminal domain, of DnaG is important for the interaction with the exosome. rRNA-derived transcripts with heteropolymeric tails are degraded faster by the exosome than their non-tailed variants Saccharolobus solfataricus