The archaeal DnaG protein needs Csl4 for binding to the exosome and enhances its interaction with adenine-rich RNAs.
The archaeal DnaG protein needs Csl4 for binding to the exosome and enhances its interaction with adenine-rich RNAs.
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DOI：
10.4161/rna.23450
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发表时间：
2013-03
期刊：
影响因子：
4.1
通讯作者：
Evguenieva-Hackenberg E
中科院分区：
文献类型：
--
作者：
Hou L;Klug G;Evguenieva-Hackenberg E
古细菌RNA降解外泌体含有一个催化活性的六聚体核心，一个由Rrp4和Csl4组成的RNA结合帽，以及一个注释为DnaG（细菌型引物酶）的蛋白质，其在RNA代谢中具有迄今未知的功能。我们发现，古细菌DnaG可以与Sulfolobus solfataricus的csl4外泌体结合，但不能与rrp4外泌体结合。体外实验表明，DnaG是一种多聚(a)结合蛋白，可促进csl4外泌体对富含腺嘌呤的转录物的降解。DnaG是S. solfataricus外胞体中除Rrp4外的第二个多聚(A)结合蛋白。这显然反映了S. solfataricus的RNA代谢需要有效和选择性地将富含腺嘌呤的RNA招募到外泌体。
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.