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The cell and stress‐specific canonical and noncanonical tRNA cleavage
Author(s) -
Rashad Sherif,
Tominaga Teiji,
Niizuma Kuniyasu
Publication year - 2021
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.30107
Subject(s) - transfer rna , angiogenin , cleavage (geology) , rna , microbiology and biotechnology , protein biosynthesis , biology , mitochondrion , cytosol , cleavage factor , biochemistry , chemistry , genetics , enzyme , gene , paleontology , fracture (geology) , angiogenesis
Following stress, transfer RNA (tRNA) is cleaved to generate tRNA halves (tiRNAs). These tiRNAs have been shown to repress protein translation. Angiogenin was considered the main enzyme that cleaves tRNA at its anticodon to generate 35–45 nucleotide long tiRNA halves, however, the recent reports indicate the presence of angiogenin‐independent cleavage. We previously observed tRNA cleavage pattern occurring away from the anticodon site. To explore this noncanonical cleavage, we analyze tRNA cleavage patterns in rat model of ischemia–reperfusion and in two rat cell lines. In vivo mitochondrial tRNAs were prone to this noncanonical cleavage pattern. In vitro, however, cytosolic and mitochondrial tRNAs could be cleaved noncanonically. Our results show an important regulatory role of mitochondrial stress in angiogenin‐mediated tRNA cleavage. Neither angiogenin nor RNH1 appear to regulate the noncanonical tRNA cleavage. Finally, we verified our previous findings of the role of Alkbh1 in regulating tRNA cleavage and its impact on noncanonical tRNA cleavage.