RNase P and RNase MRP complexes in Drosophila melanogaster

Ribonuclease P removes the 5' leader from precursor tRNAs. Nuclear RNase P is a ribonucleoprotein whose catalytic RNA (RNaseP:RNA) is bound by several proteins; the related RNase MRP shares most of these proteins but has its own RNA (RNaseMRP:RNA) and cleaves other substrates, including pre-rRNA. In mitochondria, tRNA 5' processing is carried out by a protein-only RNase P made of a tRNA methyltransferase subunit (rswl, MRPP1 homolog), a short-chain dehydrogenase subunit (scu, MRPP2/HSD17B10 homolog) and the PRORP-type nuclease subunit (mldr).

Parts follow FlyBase groups RNASEP-N, RNASEMRP and RNASEP-M. Nuclear RNase P and RNase MRP share Pop1, Pop4, Pop5, Rpp14a, Rpp14b, Rpp20, Rpp25 and Rpp30; FlyBase lists Rpp21 only in RNase P. The catalytic RNAs (RNaseP:RNA, RNaseMRP:RNA) are grounded to FlyBase gene ids. The ribonuclease activities are assigned to the whole nuclear complexes because the RNA subunit is catalytic; in the mitochondrial complex only the nuclease subunit (mldr) is given an activity. Substrate specificity of Drosophila RNase MRP has not been characterized directly and is inferred from other eukaryotes. FlyBase groups realized by this module: RNASEP (FBgg0001673), RNASEMRP (FBgg0001676). Subgroups folded into it: RNASEP-M, RNASEP-N. Participants were generated from the FlyBase gene-group membership and mapped to UniProtKB by projects/FLYBASE_GENE_GROUPS/generate_modules.py from module_specs/dmel_rnase_p_mrp.yaml. Genes without a usable UniProtKB entry are grounded to their FlyBase gene ids: RNaseMRP:RNA, RNaseP:RNA. Member genes with a gene review in this repository: scu.