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.

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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

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article

Identification of RMP24 and RMP64, human ribonuclease MRP-specific protein components

Hong Luo, Rui Che, M. Yazdan Panah, Xiaotong Chen et al.
4 citations
Cell Reports
RNA and protein synthesis mechanisms
3.22
article

Identification of RMP24 and RMP64, human ribonuclease MRP-specific protein components

Hong Luo, Rui Che, M. Yazdan Panah, Xiaotong Chen, Bhoomi Mirani, Andrei Alexandrov
article en
4 citations

Abstract

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.

Cell ReportsVol. 44(6)
Clemson University (US)
National Institutes of Health, National Institute of General Medical Sciences
Zero hunger
Openalex Percentile: Top 8%
RNA and protein synthesis mechanisms
3.22
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Identification of RMP24 and RMP64, human ribonuclease MRP-specific protein components — Hong Luo, Rui Che, et al. · Cell Reports (2025) | TGRS Research Map | TGRS