Selective Cleavage at CCA Ends and Anticodon Loops of tRNAs by Stress-Induced RNases
Stress-induced tRNA cleavage has been implicated in various cellular processes, where tRNA fragments play diverse regulatory roles. Angiogenin (ANG), a member of the RNase A superfamily, induces cleavage of tRNAs resulting in the formation of tRNA-derived stress-induced RNAs (tiRNAs) that contribute...
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Published in | Frontiers in molecular biosciences Vol. 9; p. 791094 |
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Abstract | Stress-induced tRNA cleavage has been implicated in various cellular processes, where tRNA fragments play diverse regulatory roles. Angiogenin (ANG), a member of the RNase A superfamily, induces cleavage of tRNAs resulting in the formation of tRNA-derived stress-induced RNAs (tiRNAs) that contribute to translational reprogramming aiming at cell survival. In addition to cleaving tRNA anticodon loops, ANG has been shown to cleave 3'-CCA termini of tRNAs
, although it is not known whether this process occurs in cells. It has also been suggested that tiRNAs can be generated independently of ANG, although the role of other stress-induced RNases in tRNA cleavage is poorly understood. Using gene editing and biochemical approaches, we examined the involvement of ANG in stress-induced tRNA cleavage by focusing on its cleavage of CCA-termini as well as anticodon loops. We show that ANG is not responsible for CCA-deactivation under sodium arsenite (SA) treatment
, and although ANG treatment significantly increases 3'-tiRNA levels in cells, the majority of 3'-tiRNAs retain their 3'-CCA termini. Instead, other RNases can cleave CCA-termini in cells, although with low efficiency. Moreover, in the absence of ANG, other RNases are able to promote the production of tiRNAs in cells. Depletion of RNH1 (an endogenous inhibitor of RNase A superfamily) promotes constitutively-produced tiRNAs and CCA-deactivated tRNAs in cells. Interestingly, SA treatment in RNH1-depleted cells did not increase the amount of tiRNAs or CCA-deactivated tRNAs, suggesting that RNase A superfamily enzymes are largely responsible for SA-induced tRNA cleavage. We show that interplay between stress-induced RNases cause targeting tRNAs in a stress-specific manner
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AbstractList | Stress-induced tRNA cleavage has been implicated in various cellular processes, where tRNA fragments play diverse regulatory roles. Angiogenin (ANG), a member of the RNase A superfamily, induces cleavage of tRNAs resulting in the formation of tRNA-derived stress-induced RNAs (tiRNAs) that contribute to translational reprogramming aiming at cell survival. In addition to cleaving tRNA anticodon loops, ANG has been shown to cleave 3′-CCA termini of tRNAs in vitro, although it is not known whether this process occurs in cells. It has also been suggested that tiRNAs can be generated independently of ANG, although the role of other stress-induced RNases in tRNA cleavage is poorly understood. Using gene editing and biochemical approaches, we examined the involvement of ANG in stress-induced tRNA cleavage by focusing on its cleavage of CCA-termini as well as anticodon loops. We show that ANG is not responsible for CCA-deactivation under sodium arsenite (SA) treatment in cellulo, and although ANG treatment significantly increases 3′-tiRNA levels in cells, the majority of 3′-tiRNAs retain their 3′-CCA termini. Instead, other RNases can cleave CCA-termini in cells, although with low efficiency. Moreover, in the absence of ANG, other RNases are able to promote the production of tiRNAs in cells. Depletion of RNH1 (an endogenous inhibitor of RNase A superfamily) promotes constitutively-produced tiRNAs and CCA-deactivated tRNAs in cells. Interestingly, SA treatment in RNH1-depleted cells did not increase the amount of tiRNAs or CCA-deactivated tRNAs, suggesting that RNase A superfamily enzymes are largely responsible for SA-induced tRNA cleavage. We show that interplay between stress-induced RNases cause targeting tRNAs in a stress-specific manner in cellulo. Stress-induced tRNA cleavage has been implicated in various cellular processes, where tRNA fragments play diverse regulatory roles. Angiogenin (ANG), a member of the RNase A superfamily, induces cleavage of tRNAs resulting in the formation of tRNA-derived stress-induced RNAs (tiRNAs) that contribute to translational reprogramming aiming at cell survival. In addition to cleaving tRNA anticodon loops, ANG has been shown to cleave 3′-CCA termini of tRNAs in vitro , although it is not known whether this process occurs in cells. It has also been suggested that tiRNAs can be generated independently of ANG, although the role of other stress-induced RNases in tRNA cleavage is poorly understood. Using gene editing and biochemical approaches, we examined the involvement of ANG in stress-induced tRNA cleavage by focusing on its cleavage of CCA-termini as well as anticodon loops. We show that ANG is not responsible for CCA-deactivation under sodium arsenite (SA) treatment in cellulo , and although ANG treatment significantly increases 3′-tiRNA levels in cells, the majority of 3′-tiRNAs retain their 3′-CCA termini. Instead, other RNases can cleave CCA-termini in cells, although with low efficiency. Moreover, in the absence of ANG, other RNases are able to promote the production of tiRNAs in cells. Depletion of RNH1 (an endogenous inhibitor of RNase A superfamily) promotes constitutively-produced tiRNAs and CCA-deactivated tRNAs in cells. Interestingly, SA treatment in RNH1-depleted cells did not increase the amount of tiRNAs or CCA-deactivated tRNAs, suggesting that RNase A superfamily enzymes are largely responsible for SA-induced tRNA cleavage. We show that interplay between stress-induced RNases cause targeting tRNAs in a stress-specific manner in cellulo . Stress-induced tRNA cleavage has been implicated in various cellular processes, where tRNA fragments play diverse regulatory roles. Angiogenin (ANG), a member of the RNase A superfamily, induces cleavage of tRNAs resulting in the formation of tRNA-derived stress-induced RNAs (tiRNAs) that contribute to translational reprogramming aiming at cell survival. In addition to cleaving tRNA anticodon loops, ANG has been shown to cleave 3'-CCA termini of tRNAs , although it is not known whether this process occurs in cells. It has also been suggested that tiRNAs can be generated independently of ANG, although the role of other stress-induced RNases in tRNA cleavage is poorly understood. Using gene editing and biochemical approaches, we examined the involvement of ANG in stress-induced tRNA cleavage by focusing on its cleavage of CCA-termini as well as anticodon loops. We show that ANG is not responsible for CCA-deactivation under sodium arsenite (SA) treatment , and although ANG treatment significantly increases 3'-tiRNA levels in cells, the majority of 3'-tiRNAs retain their 3'-CCA termini. Instead, other RNases can cleave CCA-termini in cells, although with low efficiency. Moreover, in the absence of ANG, other RNases are able to promote the production of tiRNAs in cells. Depletion of RNH1 (an endogenous inhibitor of RNase A superfamily) promotes constitutively-produced tiRNAs and CCA-deactivated tRNAs in cells. Interestingly, SA treatment in RNH1-depleted cells did not increase the amount of tiRNAs or CCA-deactivated tRNAs, suggesting that RNase A superfamily enzymes are largely responsible for SA-induced tRNA cleavage. We show that interplay between stress-induced RNases cause targeting tRNAs in a stress-specific manner . |
Author | Lyons, Shawn M Abe, Takaaki Ivanov, Pavel Akiyama, Yasutoshi Fay, Marta M Anderson, Paul J Tomioka, Yoshihisa |
AuthorAffiliation | 1 Laboratory of Oncology , Pharmacy Practice and Sciences , Tohoku University Graduate School of Pharmaceutical Sciences , Sendai , Japan 4 Department of Biochemistry , Boston University School of Medicine , Boston , MA , United States 5 The Genome Science Institute , Boston University School of Medicine , Boston , MA , United States 7 Department of Clinical Biology and Hormonal Regulation , Tohoku University Graduate School of Medicine , Sendai , Japan 3 Department of Medicine , Harvard Medical School , Boston , MA , United States 6 Department of Medical Science , Tohoku University Graduate School of Biomedical Engineering , Sendai , Japan 2 Division of Rheumatology, Inflammation and Immunity , Brigham and Women’s Hospital , Boston , MA , United States |
AuthorAffiliation_xml | – name: 2 Division of Rheumatology, Inflammation and Immunity , Brigham and Women’s Hospital , Boston , MA , United States – name: 3 Department of Medicine , Harvard Medical School , Boston , MA , United States – name: 4 Department of Biochemistry , Boston University School of Medicine , Boston , MA , United States – name: 5 The Genome Science Institute , Boston University School of Medicine , Boston , MA , United States – name: 7 Department of Clinical Biology and Hormonal Regulation , Tohoku University Graduate School of Medicine , Sendai , Japan – name: 6 Department of Medical Science , Tohoku University Graduate School of Biomedical Engineering , Sendai , Japan – name: 1 Laboratory of Oncology , Pharmacy Practice and Sciences , Tohoku University Graduate School of Pharmaceutical Sciences , Sendai , Japan |
Author_xml | – sequence: 1 givenname: Yasutoshi surname: Akiyama fullname: Akiyama, Yasutoshi organization: Department of Medicine, Harvard Medical School, Boston, MA, United States – sequence: 2 givenname: Shawn M surname: Lyons fullname: Lyons, Shawn M organization: The Genome Science Institute, Boston University School of Medicine, Boston, MA, United States – sequence: 3 givenname: Marta M surname: Fay fullname: Fay, Marta M organization: Department of Medicine, Harvard Medical School, Boston, MA, United States – sequence: 4 givenname: Yoshihisa surname: Tomioka fullname: Tomioka, Yoshihisa organization: Laboratory of Oncology, Pharmacy Practice and Sciences, Tohoku University Graduate School of Pharmaceutical Sciences, Sendai, Japan – sequence: 5 givenname: Takaaki surname: Abe fullname: Abe, Takaaki organization: Department of Clinical Biology and Hormonal Regulation, Tohoku University Graduate School of Medicine, Sendai, Japan – sequence: 6 givenname: Paul J surname: Anderson fullname: Anderson, Paul J organization: Department of Medicine, Harvard Medical School, Boston, MA, United States – sequence: 7 givenname: Pavel surname: Ivanov fullname: Ivanov, Pavel organization: Department of Medicine, Harvard Medical School, Boston, MA, United States |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/35300117$$D View this record in MEDLINE/PubMed |
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Keywords | angiogenin stress response tRNAs CCA-terminus RNase A superfamily |
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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Edited by: Jinghao Sheng, Zhejiang University, China Timothy E. Audas, Simon Fraser University, Canada Reviewed by: Ester Boix, Universitat Autònoma de Barcelona, Spain This article was submitted to RNA Networks and Biology, a section of the journal Frontiers in Molecular Biosciences |
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Title | Selective Cleavage at CCA Ends and Anticodon Loops of tRNAs by Stress-Induced RNases |
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