title: The archaeal DnaG protein needs Csl4 for binding to the exosome and enhances its interaction with adenine-rich RNAs.
abstract: The archaeal RNA-degrading exosome contains a catalytically active hexameric core, an RNA-binding cap formed by Rrp4 and Csl4 and the protein annotated as DnaG (bacterial type primase) with so-far-unknown functions in RNA metabolism. We found that the archaeal DnaG binds to the Csl4-exosome but not to the Rrp4-exosome of Sulfolobus solfataricus. In vitro assays revealed that DnaG is a poly(A)-binding protein enhancing the degradation of adenine-rich transcripts by the Csl4-exosome. DnaG is the second poly(A)-binding protein besides Rrp4 in the heteromeric, RNA-binding cap of the S. solfataricus exosome. This apparently reflects the need for effective and selective recruitment of adenine-rich RNAs to the exosome in the RNA metabolism of S. solfataricus.
authors: Institute of Microbiology and Molecular Biology; Heinrich-Buff-Ring; Giessen, Germany.
authors: Linlin
authors: L
authors: Hou
authors: Gabriele
authors: G
authors: Klug
authors: Elena
authors: E
authors: Evguenieva-Hackenberg
mesh_terms: D000225:Adenine / Q000378:metabolism; D019843:Archaeal Proteins / Q000235:genetics / Q000378:metabolism*; D019915:DNA Primase / Q000235:genetics / Q000378:metabolism*; D063326:Exosome Multienzyme Ribonuclease Complex / Q000378:metabolism; D011061:Poly A / Q000378:metabolism*; D019642:RNA, Archaeal / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity; D048229:Sulfolobus solfataricus / Q000235:genetics / Q000378:metabolism*
chemical_list: D019843:Archaeal Proteins; D019642:RNA, Archaeal; D016601:RNA-Binding Proteins; D011061:Poly A; D019915:DNA Primase; D063326:Exosome Multienzyme Ribonuclease Complex; D000225:Adenine
keywords: DnaG; RNA binding; archaea; exosome; poly(A) binding