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8-component RNase P (RNA plus proteins Pop1, Pop4, Pop5, Pop6, Pop7, Pop8, Rpp1). Protein Pop1 is required for the catalytic RNA activation and is positioned to provide a major contribution to its global fold, and, simultaneously, to potentially contribute to both substrate binding and the organization of the catalytic core. Proteins Pop6, Pop7 appear to be structural subunits that, together with the specialized RNA domain P3, form an interface for the Pop1 binding, while Pop8 is required for the proper interactions between Pop1 and proteins shared with the archaeal enzymes, Rpp1/Pop5. Proteins Pop6, Pop7, and Pop8 do not affect the position of the pre-tRNA substrate cleavage site, but increase the activity and stability of the RNP. Proteins Rpp1, Pop5 are required for RNA activation, and bind in the immediate vicinity of the RNA based catalytic core. In addition, Rpp1, Pop5 affect the specificity domain of yeast RNase P RNA, and are required for the engagement of Pop4. Pop4 binding affects a phylogenetically conserved part of RNase PRNA that is directly involved in substrate recognition in bacteria, and increases the level of RNase P activity. Pop4 does not affect the location of the cleavage site in the pre-tRNA substrate and is not absolutely required for the activation of the catalytic RNA |
Saccharomyces cerevisiae |