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Review
. 2024 May 9;22(1):qzae016.
doi: 10.1093/gpbjnl/qzae016.

RNase P: Beyond Precursor tRNA Processing

Peipei Wang  1 , Juntao Lin  1   2 , Xiangyang Zheng  3 , Xingzhi Xu  1
Affiliations
Review

RNase P: Beyond Precursor tRNA Processing

Peipei Wang et al. Genomics Proteomics Bioinformatics. .

Abstract

Ribonuclease P (RNase P) was first described in the 1970's as an endoribonuclease acting in the maturation of precursor transfer RNAs (tRNAs). More recent studies, however, have uncovered non-canonical roles for RNase P and its components. Here, we review the recent progress of its involvement in chromatin assembly, DNA damage response, and maintenance of genome stability with implications in tumorigenesis. The possibility of RNase P as a therapeutic target in cancer is also discussed.

Keywords: Chromatin assembly; DNA damage response; Genome stability; RNase P; Tumorigenesis.

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Conflict of interest statement

The authors have declared no competing interests.

Figures

Figure 1
Figure 1
Schematic showing stabilization of RNase P during the processing of pre-tRNA 5′ leader sequences A. pre-tRNA model with 5′ leader (indicated in red). B. Model of human H1 RNA. The C and S domains are divided by the dashed line. C. Ten RPPs wrap around H1 RNA and pre-tRNA to ensure pre-tRNA processing. C, catalytic; S, specificity; tRNA, transfer RNA; RNase P, ribonuclease P; pre-tRNA, precursor tRNA; RPP, RNase P protein.
Figure 2
Figure 2
RNase P is recruited to DNA DSBs and represses H3.3 recruitment to actively transcribed genes RPP21 and RPP29 are recruited to DNA DSBs by binding to PAR moieties, while H1 RNA may provide a potential platform for the further recruitment of downstream HR repair proteins. RPP29 represses H3.3 incorporation into actively transcribed genes by regulating H3K9me3 and H3K27me3. DSB, double-strand break; PAR, poly(ADP-ribose) polymer; HR, homologous recombination.
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