3′-processing of yeast tRNA<sup>Trp</sup> precedes 5′-processing

Kufel, Joanna; Tollervey, David

doi:10.1261/rna.2145103

Cited by 41 publications

(36 citation statements)

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“…In contrast, in cells lacking Rrp6 and, more visibly, Trz1 and both Rrp6 and Rex2, the increased level of some 5 ′ /3 ′ -ptRNAs, symptomatic of the defect in 5 ′ -end processing, was also detected. Although inhibition of 3 ′ cleavage when RNase P processing is reduced has been observed repeatedly (Lee et al 1991;Lygerou et al 1994;Kufel and Tollervey 2003), the reverse has not been reported. Moreover, tRNase Z has been shown to efficiently cleave only 5 ′ -processed pre-tRNAs, and human tRNase Z activity in vitro is inhibited by the presence of longer 5 ′ extensions (Kunzmann et al 1998;Nashimoto et al 1999;Schierling et al 2002;Dubrovsky et al 2004).…”

Section: Discussionmentioning

confidence: 96%

“…This has been demonstrated, for example, in S. cerevisiae, where mutations in RNase P block maturation of both 5 ′ and 3 ′ ends (Lee et al 1991;O'Connor and Peebles 1991;Furter et al 1992;Lygerou et al 1994). Nevertheless, several exceptions to this order of processing have been reported, including some tRNAs in mouse and wheat germ extracts (Rooney and Harding 1986;Arends and Schön 1997), and in vivo processing of yeast tRNA Trp (Kufel and Tollervey 2003). tRNA splicing and end processing are not strictly ordered, but in yeast wild-type cells, the rate of splicing is slower, and the presence 3 of the 5 ′ leader has been reported to slow down intron removal; therefore, mainly unspliced and end-processed intermediates are detected (O'Connor and Peebles 1991; Kufel and Tollervey 2003;Hiley et al 2005).…”

Section: Introductionmentioning

confidence: 98%

“…Nevertheless, several exceptions to this order of processing have been reported, including some tRNAs in mouse and wheat germ extracts (Rooney and Harding 1986;Arends and Schön 1997), and in vivo processing of yeast tRNA Trp (Kufel and Tollervey 2003). tRNA splicing and end processing are not strictly ordered, but in yeast wild-type cells, the rate of splicing is slower, and the presence 3 of the 5 ′ leader has been reported to slow down intron removal; therefore, mainly unspliced and end-processed intermediates are detected (O'Connor and Peebles 1991; Kufel and Tollervey 2003;Hiley et al 2005). This could also be related to the site of pre-tRNA splicing outside of the nucleus.…”

Section: Introductionmentioning

confidence: 99%

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tRNA 3′ processing in yeast involves tRNase Z, Rex1, and Rrp6

Skowronek

Grzechnik

Späth

et al. 2013

RNA

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Mature tRNA 3 ′ ends in the yeast Saccharomyces cerevisiae are generated by two pathways: endonucleolytic and exonucleolytic. Although two exonucleases, Rex1 and Rrp6, have been shown to be responsible for the exonucleolytic trimming, the identity of the endonuclease has been inferred from other systems but not confirmed in vivo. Here, we show that the yeast tRNA 3 ′ endonuclease tRNase Z, Trz1, is catalyzing endonucleolytic tRNA 3 ′ processing. The majority of analyzed tRNAs utilize both pathways, with a preference for the endonucleolytic one. However, 3′ -end processing of precursors with long 3 ′ trailers depends to a greater extent on Trz1. In addition to its function in the nucleus, Trz1 processes the 3 ′ ends of mitochondrial tRNAs, contributing to the general RNA metabolism in this organelle.

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Section: Discussionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

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tRNA 3′ processing in yeast involves tRNase Z, Rex1, and Rrp6

Skowronek

Grzechnik

Späth

et al. 2013

RNA

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“…Saturation of RNase P RNA Is Not a Reason for Pre-tRNA Accumulation in the Absence of Maf1-First, we explored the possibility that accumulation of untrimmed initial transcripts in maf1⌬ cells is due to saturation of RNase P, which removes the 5Ј leader preceding removal of the 3Ј trailer (40). RPR1, the gene encoding the RNA subunit of RNase P, is transcribed by Pol III (41).…”

Section: Accumulation Of Pre-trna Is Correlated With Loss Of Nuclearmentioning

confidence: 99%

Maf1 Protein, Repressor of RNA Polymerase III, Indirectly Affects tRNA Processing

Karkusiewicz

Turowski

Graczyk

et al. 2011

Journal of Biological Chemistry

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Maf1 is negative regulator of RNA polymerase III in yeast. We observed high levels of both primary transcript and end-matured, intron-containing pre-tRNAs in the maf1⌬ strain. This pre-tRNA accumulation could be overcome by transcription inhibition, arguing against a direct role of Maf1 in tRNA maturation and suggesting saturation of processing machinery by the increased amounts of primary transcripts. Saturation of the tRNA exportin, Los1, is one reason why end-matured introncontaining pre-tRNAs accumulate in maf1⌬ cells. However, it is likely possible that other components of the processing pathway are also limiting when tRNA transcription is increased. According to our model, Maf1-mediated transcription control and nuclear export by Los1 are two major stages of tRNA biosynthesis that are regulated by environmental conditions in a coordinated manner.

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“…In eukaryotes, tRNAs are transcribed in the nucleus as primary transcripts that undergo extensive processing, chemical modification, and subcellular trafficking to produce the mature tRNAs that function in cytoplasmic translation. In the yeast Saccharomyces cerevisiae, tRNA transcription in the nucleolus (1), with one exception (2), is followed by removal of the 5′ leader sequence by RNase P (3). The 3′ trailer is subsequently removed endonucleolytically, presumably by tRNase Z (4-6), and/or exonucleolytically by Rex1 (7,8).…”

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confidence: 99%

Retrograde transfer RNA nuclear import provides a new level of tRNA quality control in Saccharomyces cerevisiae

Kramer

Hopper

2013

Proc. Natl. Acad. Sci. U.S.A.

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In eukaryotes, transfer RNAs (tRNAs) are transcribed in the nucleus yet function in the cytoplasm; thus, tRNA movement within the cell was believed to be unidirectional-from the nucleus to the cytoplasm. It is now known that mature tRNAs also move in a retrograde direction from the cytoplasm to the nucleus via retrograde tRNA nuclear import, a process that is conserved from yeast to vertebrates. The biological significance of this tRNA nuclear import is not entirely clear. We hypothesized that retrograde tRNA nuclear import might function in proofreading tRNAs to ensure that only proper tRNAs reside in the cytoplasm and interact with the translational machinery. Here we identify two major types of aberrant tRNAs in yeast: a 5′, 3′ end-extended, spliced tRNA and hypomodified tRNAs. We show that both types of aberrant tRNAs accumulate in mutant cells that are defective in tRNA nuclear traffic, suggesting that they are normally imported into the nucleus and are repaired or degraded. The retrograde pathway functions in parallel with the cytoplasmic rapid tRNA decay pathway previously demonstrated to monitor tRNA quality, and cells are not viable if they lack both pathways. Our data support the hypothesis that the retrograde process provides a newly discovered level of tRNA quality control as a pathway that monitors both end processing of pre-tRNAs and the modification state of mature tRNAs.tRNA retrograde pathway | tRNA processing errors | quality control pathways | Mtr10 | Los1 T ransfer RNAs (tRNAs) are well known for their role as adaptor molecules during the translation of mRNAs into proteins, delivering amino acids to the ribosome for incorporation into a polypeptide chain. In eukaryotes, tRNAs are transcribed in the nucleus as primary transcripts that undergo extensive processing, chemical modification, and subcellular trafficking to produce the mature tRNAs that function in cytoplasmic translation. In the yeast Saccharomyces cerevisiae, tRNA transcription in the nucleolus (1), with one exception (2), is followed by removal of the 5′ leader sequence by RNase P (3). The 3′ trailer is subsequently removed endonucleolytically, presumably by tRNase Z (4-6), and/or exonucleolytically by Rex1 (7,8). Following removal of the 3′ trailer, the nucleotides C 74 C 75 A 76 , necessary for tRNA aminoacylation, are added to the 3′ terminus. Twenty percent of yeast tRNAs are transcribed with an intron (9). Splicing of tRNA introns occurs in the cytoplasm in yeast, on the outer surface of mitochondria where the tRNA splicing endonuclease complex resides (10-12). Thus, end-processed intron-containing tRNAs are exported from the nucleus to the cytoplasm before removal of the intron. This primary export of intron-containing pre-tRNA is mediated by the β-importin family member Los1 (13-15). Because LOS1 is unessential and because it is essential to have tRNAs delivered to the cytoplasm, there is at least one additional unidentified nuclear exporter for end-processed intron-containing pre-tRNA (16).tRNAs are subject to numerous pos...

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3′-processing of yeast tRNA^Trp precedes 5′-processing

Cited by 41 publications

References 46 publications

tRNA 3′ processing in yeast involves tRNase Z, Rex1, and Rrp6

tRNA 3′ processing in yeast involves tRNase Z, Rex1, and Rrp6

Maf1 Protein, Repressor of RNA Polymerase III, Indirectly Affects tRNA Processing

Retrograde transfer RNA nuclear import provides a new level of tRNA quality control in Saccharomyces cerevisiae

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3′-processing of yeast tRNATrp precedes 5′-processing

Cited by 41 publications

References 46 publications

tRNA 3′ processing in yeast involves tRNase Z, Rex1, and Rrp6

tRNA 3′ processing in yeast involves tRNase Z, Rex1, and Rrp6

Maf1 Protein, Repressor of RNA Polymerase III, Indirectly Affects tRNA Processing

Retrograde transfer RNA nuclear import provides a new level of tRNA quality control in Saccharomyces cerevisiae

Contact Info

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3′-processing of yeast tRNA^Trp precedes 5′-processing