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Updated: Sep 20, 2025

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

Rui Che1, Bhoomi Mirani1, Monireh Panah1

  • 1Department of Genetics and Biochemistry, Clemson University, Clemson, SC 29631, USA; Clemson University Center for Human Genetics, Greenwood, SC 29646, USA.

Cell Reports
|May 25, 2025
PubMed

Insights

Researchers identified two new proteins, RMP24 and RMP64, essential for human RNase MRP function in precursor rRNA processing. These findings reveal unique protein components of this crucial ribonucleoprotein enzyme.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Human RNase MRP is a ribonucleoprotein (RNP) enzyme crucial for precursor rRNA (pre-rRNA) processing.
  • It is related to RNase P, sharing some protein subunits but differing in catalytic RNAs and specific proteins.
  • The specific protein components of human RNase MRP have remained unidentified.

Purpose of the Study:

  • To identify the unique protein subunits of human RNase MRP.
  • To characterize the function of these novel subunits in pre-rRNA processing.

Main Methods:

  • Genome-wide forward genetic screening was employed to identify candidate genes.
  • Functional assays were performed to assess the role of identified genes in pre-rRNA processing.
  • Co-immunoprecipitation was used to determine protein-RNA associations.

Main Results:

  • Two previously uncharacterized human genes, RMP24 and RMP64, were identified.
  • RMP24 and RMP64 are essential for pre-rRNA processing at ITS1 site 2.
  • These proteins associate with MRP RNA but not with RNase P-specific H1 RNA.
  • RMP24 and RMP64 show predicted structural similarities to yeast RNase MRP-specific proteins.

Conclusions:

  • RMP24 and RMP64 are unique protein components of human nuclear RNase MRP.
  • These findings elucidate the composition of a key ribonucleoprotein enzyme involved in ribosome biogenesis.
Keywords:
CP: Molecular biologyCRISPR screeningforward geneticshigh-throughput screeningribonuclease P/MRPstructure

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