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Stress induces tRNA cleavage by angiogenin in mammalian cells
Author(s) -
Fu Hanjiang,
Feng Junjun,
Liu Qin,
Sun Fang,
Tie Yi,
Zhu Jie,
Xing Ruiyun,
Sun Zhixian,
Zheng Xiaofei
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.12.043
Subject(s) - angiogenin , transfer rna , rnase p , cleavage (geology) , nuclease , protein biosynthesis , microbiology and biotechnology , rna , biology , translation (biology) , amino acid , in vitro , biochemistry , chemistry , angiogenesis , messenger rna , dna , genetics , gene , paleontology , fracture (geology)
tRNAs play a central role in protein translation, acting as the carrier of amino acids. By cloning microRNAs, we unexpectedly obtained some tRNA fragments generated by tRNA cleavage in the anticodon loop. These tRNA fragments are present in many cell lines and different mouse tissues. In addition, various stress conditions can induce this tRNA cleavage event in mammalian cells. More importantly, angiogenin (ANG), a member of RNase A superfamily, appears to be the nuclease which cleaves tRNAs into tRNA halves in vitro and in vivo. These results imply that angiogenin plays an important physiological role in cell stress response, except for the known function of inducing angiogenesis.

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