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Footprinting analysis demonstrates extensive similarity between eukaryotic RNase P and RNase MRP holoenzymes
Author(s) -
Olga Esakova,
Anna Perederina,
Chao Quan,
Mark E. Schmitt,
Andrey S. Krasilnikov
Publication year - 2008
Publication title -
rna
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.037
H-Index - 171
eISSN - 1469-9001
pISSN - 1355-8382
DOI - 10.1261/rna.1106408
Subject(s) - rnase mrp , rnase p , biology , rnase ph , rna , exosome complex , footprinting , rnase h , degradosome , biochemistry , ribonuclease , transfer rna , non coding rna , ribonuclease iii , microbiology and biotechnology , gene , transcription factor , rna interference
Eukaryotic ribonuclease (RNase) P and RNase MRP are evolutionary related RNA-based enzymes involved in metabolism of various RNA molecules, including tRNA and rRNA. In contrast to the closely related eubacterial RNase P, which is comprised of an RNA component and a single small protein, these enzymes contain multiple protein components. Here we report the results of footprinting studies performed on purified Saccharomyces cerevisiae RNase MRP and RNase P holoenzymes. The results identify regions of the RNA components affected by the protein moiety, suggest a role of the proteins in stabilization of the RNA fold, and point to substantial similarities between the two evolutionary related RNA-based enzymes.

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