Identification of RMP24 and RMP64, human ribonuclease MRP-specific protein components
Human RNase MRP is a ribonucleoprotein (RNP) enzyme that processes precursor rRNA (pre-rRNA) at ITS1 site 2 and may have additional activities. It is an endonuclease related to RNase P, which processes pre-tRNAs and pre-tRNA-like substrates. In Saccharomyces cerevisiae, these two RNPs utilize distinct catalytic RNAs with eight shared and one or two specific protein subunits. However, the human RNase MRP-specific protein subunits remain unidentified. Our genome-wide forward genetic screening identifies two poorly characterized human genes, which we name ribonuclease MRP subunit P24 (RMP24) and RMP64. We show that Rmp24 and Rmp64 are required for pre-rRNA ITS1 site 2 processing and associate with MRP RNA but are not required for RNase P activity and do not associate with RNase P-specific H1 RNA. Despite limited sequence homology, Rmp24 and Rmp64 exhibit predicted structural similarities to two RNase MRP-specific components in S. cerevisiae. Collectively, our functional screening and validation reveal two protein components unique to human nuclear RNase MRP.
Authors
- Hong Luo (ORCID: https://orcid.org/0000-0001-9223-1786)
- Rui Che (ORCID: https://orcid.org/0000-0001-5195-9260)
- M. Yazdan Panah
- Xiaotong Chen (ORCID: https://orcid.org/0000-0003-0836-6229)
- Bhoomi Mirani
- Andrei Alexandrov
Institutions
- Clemson University (US)
Publication Details
- Journal
- Cell Reports
- Published
- 2025-05-24
- DOI
- https://doi.org/10.1016/j.celrep.2025.115752
- Citations
- 4
- Primary Topic
- RNA and protein synthesis mechanisms
- Type
- article
- Field-Weighted Citation Impact
- 3.22
Funders
- National Institutes of Health
- National Institute of General Medical Sciences