期刊
MOLECULAR GENETICS AND GENOMICS
卷 286, 期 5-6, 页码 359-369出版社
SPRINGER HEIDELBERG
DOI: 10.1007/s00438-011-0651-y
关键词
RNase P diversity; Prasinophyte; pre-tRNA processing
资金
- Ministerio de Ciencia e Innovacion, Spain
- European Regional Fund [BFU2007-60651]
- Junta de Andalucia, Spain [P06-CVI-01692]
- European Union [227799]
- National Science Foundation [MCB-0238233, MCB-0843543]
RNase P catalyzes 5'-maturation of tRNAs. While bacterial RNase P comprises an RNA catalyst and a protein cofactor, the eukaryotic (nuclear) variant contains an RNA and up to ten proteins, all unrelated to the bacterial protein. Unexpectedly, a nuclear-encoded bacterial RNase P protein (RPP) homolog is found in several prasinophyte algae including Ostreococcus tauri. We demonstrate that recombinant O. tauri RPP can functionally reconstitute with bacterial RNase P RNAs (RPRs) but not with O. tauri organellar RPRs, despite the latter's presumed bacterial origins. We also show that O. tauri PRORP, a homolog of Arabidopsis PRORP-1, displays tRNA 5'-processing activity in vitro. We discuss the implications of the striking diversity of RNase P in O. tauri, the smallest known free-living eukaryote.
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