例如:"lncRNA", "apoptosis", "WRKY"

Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP.

RNA. 2011 Oct;17(10):1922-31. Epub 2011 Aug 30
Anna Perederina 1 , Elena Khanova , Chao Quan , Igor Berezin , Olga Esakova , Andrey S Krasilnikov
Anna Perederina 1 , Elena Khanova , Chao Quan , Igor Berezin , Olga Esakova , Andrey S Krasilnikov
+ et al

[No authors listed]

Author information
  • 1 Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA16802, USA.

摘要


Ribonuclease (RNase) MRP is a multicomponent ribonucleoprotein complex closely related to RNase P. RNase MRP and eukaryotic RNase P share most of their protein components, as well as multiple features of their catalytic RNA moieties, but have distinct substrate specificities. While RNase P is practically universally found in all three domains of life, RNase MRP is essential in eukaryotes. The structural organizations of eukaryotic RNase P and RNase MRP are poorly understood. Here, we show that Pop5 and Rpp1, protein components found in both RNase P and RNase MRP, form a heterodimer that binds directly to the conserved area of the putative catalytic domain of RNase MRP RNA. The Pop5/Rpp1 binding site corresponds to the protein binding site in bacterial RNase P RNA. Structural and evolutionary roles of the Pop5/Rpp1 heterodimer in RNases P and MRP are discussed.