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Literature summary for 2.7.7.101 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
Search for more literature for 2.7.7.101

Cloned(Commentary)

Cloned (Comment) Organism
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

Protein Variants Comment Organism
E175Q site-directed mutagenesis of the TOPRIM domain, DnaGE175Q has a poly(rA) preference like wild-type DnaG Saccharolobus solfataricus
K6A/Y7A site-directed mutagenesis of the N-terminal domain Saccharolobus solfataricus
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

Metals/Ions Comment Organism Structure
Mg2+ required Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus P95980 gene dnaG
-

Purification (Commentary)

Purification (Comment) Organism
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

Subunits Comment Organism
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

Synonyms Comment Organism
DnaG
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

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

pH Optimum

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

General Information

General Information Comment Organism
evolution phylogenetic analysis of DnaG proteins in archaea, overview Saccharolobus solfataricus
additional information comparison of bacterial and archaeal DnaG and composition of reconstituted Sulfolobus solfataricus exosomes, overview Saccharolobus solfataricus
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