The human tRNA-modifying protein, TRIT1, forms amyloid fibers in vitro

Waller, Thomas J.; Read, David F.; Engelke, David R.; Smaldino, Philip J.

doi:10.1016/j.gene.2016.10.041

Cited by 11 publications

(5 citation statements)

References 17 publications

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“…TRIT1 modification alters structure stability, ribosome interactions, and translation efficacy (13,27,28). TRIT1 has also been implicated in tRNA gene-mediated transcriptional silencing (26), in amyloid fiber folding (29), as a tumor suppressor (30), and in selenoprotein regulation (31). Selenoproteins are responsible for thyroid hormone homeostasis (32).…”

Section: Discussionmentioning

confidence: 99%

Canis familiaris tissues are characterized by different profiles of cytokinins typical of the tRNA degradation pathway

Seegobin

Kisiała

Noble³

et al. 2018

FASEB j.

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Cytokinins (CKs) are a group of phytohormones essential to plant growth and development. The presence of these N-modified adenine derivatives has also been documented in other groups of organisms, including bacteria, fungi, and insects. Thus far, however, only a single CK, N-(Δ-isopentenyl) adenine-9-riboside (iPR), has been identified in mammals. In plants, the nucleotide form of isopentenyladenine [iPR (either mono-, di-, or tri-) phosphate (iPRP)] is the first form of CK synthesized, and it is further modified to produce other CK types. To determine if a similar biosynthesis pathway exists in mammals, we tested for the presence of 27 CKs in a wide selection of canine organs using HPLC electrospray ionization-tandem mass spectrometry. Seven forms of CK were detected in the majority of the analyzed samples, including iPR, iPRP, cis-zeatin-9-riboside, cis-zeatin-9-riboside-5' (either mono-, di-, or triphosphate), 2-methylthio-N-isopentenyladenine, 2-methylthio-N-isopentenyladenosine, and 2-methylthio-zeatin. Total CK concentrations ranged from 1.96 pmol/g fresh weight (adrenal glands) to 1.40 × 10 pmol/g fresh weight (thyroid). The results of this study provide evidence that mammalian cells, like plant cells, can synthesize and process a diverse set of CKs including cis- and methylthiol-type CKs.-Seegobin, M., Kisiala, A., Noble, A., Kaplan, D., Brunetti, C., Emery, R. J. N. Canis familiaris tissues are characterized by different profiles of cytokinins typical of tRNA degradation pathway.

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Section: Discussionmentioning

confidence: 99%

Canis familiaris tissues are characterized by different profiles of cytokinins typical of the tRNA degradation pathway

Seegobin

Kisiała

Noble³

et al. 2018

FASEB j.

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“…tRNA-isopentenyltransferase 1 (TRIT1), a homolog of the prokaryotic miaA, facilitates production of tRNA-bound iP-type CKs in human cytosol and mitochondria (Lamichhane et al, 2013;Smaldino et al, 2015). TRIT1 was previously suggested to play a role as a tumor suppressor (Spinola et al, 2005), in selenoprotein regulation (Fradejas et al, 2013) in gene-mediated transcriptional silencing (Smaldino et al, 2015) and amyloid fiber folding (Waller et al, 2017). The product of the TRIT1 gene, iPR, has long been the lone CK type detected as tRNA-bound or as a free mononucleotide in mammals (Persson et al, 1994;Golovko et al, 2000).…”

Section: The Steps Of 2mes-ck Production Via the Trna Degradation Patmentioning

confidence: 99%

The Origins and Roles of Methylthiolated Cytokinins: Evidence From Among Life Kingdoms

Gibb

Kisiała

Morrison

et al. 2020

Front. Cell Dev. Biol.

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“…Suzuki and colleagues originally reported that aggregated Mod5 in the cytoplasm conveys resistance to certain fungicides [29], which might be consistent with the property having evolved in fungi to provide a reserve population of yeast that are resistant to antifungal attack. Interestingly, the human orthologue, TRIT1, has retained both the cytoplasmic and nuclear functions of Mod5 [22], and we recently demonstrated that it retains the amyloid fibril formation potential of Mod5 [34]. It is not clear why fibril formation would have been retained in an organism as distant from fungi as humans if cytoplasmic aggregation were the selective pressure, although it is possible that this method of removing Mod5 might regulate cholesterol biosynthesis or protein prenylation by modulating the availability of substrates.…”

Section: Discussionmentioning

confidence: 99%

Aggregation of Mod5 is affected by tRNA binding with implications for tRNA gene‐mediated silencing

et al. 2017

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Mod5 is a multifunctional protein that modifies a subset of tRNAs in the cytoplasm and is also required for an RNA-mediated form of transcriptional silencing. Previous in vivo studies have shown that the nuclear silencing function of Mod5 does not require that the causative tRNA gene encode a Mod5 substrate, though Mod5 is still required. However, previous data have not directly tested whether Mod5 can directly bind substrate and nonsubstrate RNAs. We herein demonstrate that Mod5 directly binds to both substrate and nonsubstrate RNAs, including a highly structured, non-tRNA sequence (5S-rRNA), consistent with previous in vivo data. Furthermore, we show that some RNAs drastically change the aggregation behavior of Mod5 with implications for tRNA-gene mediated silencing.

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The human tRNA-modifying protein, TRIT1, forms amyloid fibers in vitro

Cited by 11 publications

References 17 publications

Canis familiaris tissues are characterized by different profiles of cytokinins typical of the tRNA degradation pathway

Canis familiaris tissues are characterized by different profiles of cytokinins typical of the tRNA degradation pathway

The Origins and Roles of Methylthiolated Cytokinins: Evidence From Among Life Kingdoms

Aggregation of Mod5 is affected by tRNA binding with implications for tRNA gene‐mediated silencing

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