Loss of the mitochondrial protein-only ribonuclease P complex causes aberrant tRNA processing and lethality in Drosophila

Sen, Aditya; Karasik, Agnes; Shanmuganathan, Aranganathan; Mirkovic, Elena; Koutmos, Markos; Cox, Rachel T.

doi:10.1093/nar/gkw338

Cited by 32 publications

(50 citation statements)

References 63 publications

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“…In Drosophila , small interfering RNA (siRNA)-mediated knockdown of the MTase performing the m 1 A9 modification was shown to be embryonically lethal [32]. In HeLa cells, the knockdown resulted in reduced mitochondrial respiration [33], indicating that this enzyme is also important for cell viability.…”

Section: The Biological Role Of M1a Modifications In Trnamentioning

confidence: 99%

m1A Post‐Transcriptional Modification in tRNAs

et al. 2017

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To date, about 90 post-transcriptional modifications have been reported in tRNA expanding their chemical and functional diversity. Methylation is the most frequent post-transcriptional tRNA modification that can occur on almost all nitrogen sites of the nucleobases, on the C5 atom of pyrimidines, on the C2 and C8 atoms of adenosine and, additionally, on the oxygen of the ribose 2′-OH. The methylation on the N1 atom of adenosine to form 1-methyladenosine (m1A) has been identified at nucleotide position 9, 14, 22, 57, and 58 in different tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. This review provides an overview of the currently known m1A modifications, the different m1A modification sites, the biological role of each modification, and the enzyme responsible for each methylation in different species. The review further describes, in detail, two enzyme families responsible for formation of m1A at nucleotide position 9 and 58 in tRNA with a focus on the tRNA binding, m1A mechanism, protein domain organisation and overall structures.

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Section: The Biological Role Of M1a Modifications In Trnamentioning

confidence: 99%

m1A Post‐Transcriptional Modification in tRNAs

et al. 2017

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“…Recessive mutations in human TRMET10C, a subunit of human mitochondrial RNase P [96], cause defects in mitochondrial RNA processing and multiple respiratory chain deficiencies [141]. In Drosophila , loss of the mitochondrial RNase P subunit is lethal [142]. …”

Section: Functions Of Modified Nucleosides Synthesized By Spout Trmentioning

confidence: 99%

Transfer RNA methyltransferases with a SpoU‐TrmD (SPOUT) fold and their modified nucleosides in tRNA

Hori

2017

Biomolecules

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The existence of SpoU-TrmD (SPOUT) RNA methyltransferase superfamily was first predicted by bioinformatics. SpoU is the previous name of TrmH, which catalyzes the 2’-O-methylation of ribose of G18 in tRNA; TrmD catalyzes the formation of N1-methylguanosine at position 37 in tRNA. Although SpoU (TrmH) and TrmD were originally considered to be unrelated, the bioinformatics study suggested that they might share a common evolution origin and form a single superfamily. The common feature of SPOUT RNA methyltransferases is the formation of a deep trefoil knot in the catalytic domain. In the past decade, the SPOUT RNA methyltransferase superfamily has grown; furthermore, knowledge concerning the functions of their modified nucleosides in tRNA has also increased. Some enzymes are potential targets in the design of anti-bacterial drugs. In humans, defects in some genes may be related to carcinogenesis. In this review, recent findings on the tRNA methyltransferases with a SPOUT fold and their methylated nucleosides in tRNA, including classification of tRNA methyltransferases with a SPOUT fold; knot structures, domain arrangements, subunit structures and reaction mechanisms; tRNA recognition mechanisms, and functions of modified nucleosides synthesized by this superfamily, are summarized. Lastly, the future perspective for studies on tRNA modification enzymes are considered.

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“…14,15 In fact, approximately 610 tRNA genes in humans are transcribed into primary products, precursor tRNAs (pre-tRNAs), under the catalysis of RNA polymerase III (Pol III), which must then undergo a series of complex processing to transform into mature tRNAs. [17][18][19] Subsequently, a CCA sequence associated with aminoacylation will be added to the 3' end by tRNA nucleotidyltransferase 1 (TRNT1). [17][18][19] Subsequently, a CCA sequence associated with aminoacylation will be added to the 3' end by tRNA nucleotidyltransferase 1 (TRNT1).…”

Section: Structure Of Trnasmentioning

confidence: 99%

“…16 During this process, the 5' leader and 3' trailer in the pre-tRNA are removed by ribonuclease P (RNase P) and RNase Z respectively. [17][18][19] Subsequently, a CCA sequence associated with aminoacylation will be added to the 3' end by tRNA nucleotidyltransferase 1 (TRNT1). 20 Furthermore, the complete maturation of certain tRNAs needs the removal of introns between positions 37 and 38.…”

Section: Structure Of Trnasmentioning

confidence: 99%

The tRNA‐associated dysregulation in immune responses and immune diseases

et al. 2019

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Transfer RNA (tRNA), often considered as a housekeeping molecule, mainly participates in protein translation by transporting amino acids to the ribosome. Nevertheless, accumulating evidence has shown that tRNAs are closely related to various physiological and pathological processes. The proper functioning of the immune system is the key to human health. The aim of this review is to investigate the relationships between tRNAs and the immune system. We detail the biogenesis and structure of tRNAs and summarize the pathogen tRNA-mediated infection and host responses. In addition, we address recent advances in different aspects of tRNA-associated dysregulation in immune responses and immune diseases, such as tRNA molecules, tRNA modifications, tRNA derivatives and tRNA aminoacylation. Therefore, tRNAs play an important role in immune regulation. Although our knowledge of tRNAs in the context of immunity remains, for the most part, unknown, this field deserves in-depth research to provide new ideas for the treatment of immune diseases. K E Y W O R D Sbiogenesis, immune diseases, immune responses, tRNA F I G U R E 1 The biogenesis and structure of tRNAs. tRNA: Transfer RNA; Pol III: RNA polymerase III; pre-tRNA: Precursor tRNA; mRNA: Messenger RNA; aaRS: Aminoacyl-tRNA synthetase; tsRNA: tRNA-derived small RNA; tRF: tRNA-derived fragment; tiRNA: tRNA-derived stress-induced RNA

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Loss of the mitochondrial protein-only ribonuclease P complex causes aberrant tRNA processing and lethality in Drosophila

Cited by 32 publications

References 63 publications

m1A Post‐Transcriptional Modification in tRNAs

m1A Post‐Transcriptional Modification in tRNAs

Transfer RNA methyltransferases with a SpoU‐TrmD (SPOUT) fold and their modified nucleosides in tRNA

The tRNA‐associated dysregulation in immune responses and immune diseases

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