Journal article

Publication year: 2013

Pages: 415-424

Journal: RNA Biology

Volume number: 10

Issue number: 3

ISSN: 1547-6286

DOI Link: https://doi.org/10.4161/rna.23450

Publisher: Taylor and Francis Group

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.

Harvard Citation style: Hou, L., Klug, G. and Evguenieva-Hackenberg, E. (2013) The archaeal DnaG protein needs Csl4 for binding to the exosome and enhances its interaction with adenine-rich RNAs, RNA Biology, 10(3), pp. 415-424. https://doi.org/10.4161/rna.23450

APA Citation style: Hou, L., Klug, G., & Evguenieva-Hackenberg, E. (2013). The archaeal DnaG protein needs Csl4 for binding to the exosome and enhances its interaction with adenine-rich RNAs. RNA Biology. 10(3), 415-424. https://doi.org/10.4161/rna.23450