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Updated: May 29, 2025

Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip
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Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip

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Identification of Two Elusive Human Ribonuclease MRP-Specific Protein Components

Rui Che1,2, Bhoomi Mirani1,2, Monireh Panah1,2

  • 1Dept. of Genetics and Biochemistry, Clemson University, Clemson, SC 29631, USA.

Biorxiv : the Preprint Server for Biology
|February 3, 2025
PubMed

Insights

Researchers identified two new proteins, RPP24 and RPP64, essential for human Ribonuclease MRP (RNase MRP) function in pre-ribosomal RNA processing. These proteins are unique to RNase MRP and not involved in Ribonuclease P (RNase P) activity.

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Ribonuclease MRP (RNase MRP) and Ribonuclease P (RNase P) are crucial human ribonucleoprotein enzymes with shared protein components.
  • RNase MRP processes pre-ribosomal RNA (pre-rRNA) at ITS1 site 2, while RNase P cleaves pre-tRNA 5' leader sequences.
  • The specific protein constituents unique to human RNase MRP have remained largely uncharacterized.

Purpose of the Study:

  • To identify novel protein components specific to human nuclear RNase MRP.
  • To investigate the functional roles of newly identified proteins in pre-rRNA processing.
  • To differentiate the protein composition of RNase MRP from RNase P.

Main Methods:

  • Genome-wide forward genetic screening was employed to identify essential genes.
  • Functional assays were performed to assess the role of identified proteins in pre-rRNA processing.
  • Co-immunoprecipitation and structural predictions were used to analyze protein-RNA interactions and structural similarities.

Main Results:

  • Two previously poorly characterized human genes, RPP24 and RPP64, were identified and found to be essential for pre-rRNA ITS1 site 2 processing.
  • RPP24 and RPP64 proteins associate with RNA MRP but are not required for RNase P activity or association with RNA H1.
  • RPP24 and RPP64 show predicted structural similarities to yeast RNase MRP-specific components, indicating conserved structural tetapi divergent functional roles.

Conclusions:

  • RPP24 and RPP64 are the first identified protein components unique to human nuclear RNase MRP.
  • These findings expand our understanding of the distinct protein machinery of RNase MRP and RNase P.
  • The unique proteins contribute to the specific function of RNase MRP in pre-rRNA maturation.

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