The function of transfer RNAs (tRNAs) depends on enzymes that cleave primary transcript ends, add a 3′ CCA tail, introduce post‐transcriptional base modifications, and charge (aminoacylate) mature tRNAs with the correct amino acid. Maintaining an available pool of the resulting aminoacylated tRNAs is essential for protein synthesis. High‐throughput sequencing techniques have recently been developed to provide a comprehensive view of aminoacylation state in a tRNA‐specific fashion. However, these methods have never been applied to plants. Here, we treated
Protein‐only RNase P (PRORP) is an essential enzyme responsible for the 5′ maturation of precursor tRNAs (pre‐tRNAs). PRORPs are classified into three categories with unique molecular architectures, although all three classes of PRORPs share a mechanism and have similar active sites. Single subunit PRORPs, like those found in plants, have multiple isoforms with different localizations, substrate specificities, and temperature sensitivities. Most recently,
This article is categorized under: RNA Structure and Dynamics > RNA Structure, Dynamics and Chemistry RNA Structure and Dynamics > Influence of RNA Structure in Biological Systems
- PAR ID:
- 10502189
- Publisher / Repository:
- Wiley Blackwell (John Wiley & Sons)
- Date Published:
- Journal Name:
- WIREs RNA
- Volume:
- 15
- Issue:
- 2
- ISSN:
- 1757-7004
- Format(s):
- Medium: X
- Sponsoring Org:
- National Science Foundation
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