Dual function of the tRNA(m5U54)methyltransferase in tRNA maturation

Johansson, Marcus; Byström, Andeŕs S.

doi:10.1017/s1355838202027851

Cited by 77 publications

(87 citation statements)

References 39 publications

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“…The mutant gene in each of the 11 remaining groups (Table 1) was identified by complementing the phenotype with a yeast genomic library and subsequent confirmation that the original mutation was genetically linked to the locus for the complementing gene. As the sup61-T47:2C allele generates a requirement for several different tRNA modifying enzymes [5,11], we expected that the screen would identify factors involved in the modification of . In addition to trm1, tan1 and bud13 mutants, the screen identified strains with mutations in the DUS2 and MOD5 genes (Table 1) [11,12,19].…”

Section: Resultsmentioning

confidence: 99%

“…As the inactivation of any of several tRNA modifying factors in sup61-T47:2C cells causes a decreased abundance of the altered [5,11], it seemed likely that mutations in DUS2 or MOD5 would induce a similar defect. Even though the sup61 + gene is essential, we previously showed that the inviability of sup61Δ cells is suppressed by increased dosage of a gene ( tS(UGA)P ) coding for [24].…”

Section: Resultsmentioning

confidence: 99%

“…We previously identified four mutant sup61 alleles in a screen for strains that require the TRM2 gene, encoding the tRNA (m 5 U 54 ) methyltransferase, for growth [5]. The sup61 trm2 double mutants are viable at 25°C but inviable or very slow growing at 30°C.…”

Section: Introductionmentioning

confidence: 99%

“…The m 5 U 54 residue is present in and the lack of Trm2 causes decreased abundance of the altered species. In addition to the requirement for TRM2 , direct tests showed that the growth of the sup61 mutants is dependent on other enzymes that catalyze nucleoside modifications in [5]. These enzymes (Pus4, Trm1, and Trm3) are required for the formation of pseudouridine (Ψ) at position 55, N 2 , N 2 -dimethylguanosine () at position 26 and 2′-O-methylguanosine (Gm) at position 18 in tRNAs [6–8].…”

Section: Introductionmentioning

confidence: 99%

“…Similar to the absence of Trm2, the lack of Pus4, Trm1, or Trm3 causes a reduction in the levels of the altered . Moreover, introduction of a null allele of LHP1 into the sup61 mutants was found to inhibit growth and reduce the levels of the altered [5]. The Lhp1 protein promotes tRNA folding and protects the 3ʹ end of pre-tRNAs from exonucleolytic digestion [9,10].…”

Section: Introductionmentioning

confidence: 99%

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Identification of factors that promote biogenesis of tRNA_CGA^Ser

Zhou

Byström

et al. 2018

RNA Biology

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A wide variety of factors are required for the conversion of pre-tRNA molecules into the mature tRNAs that function in translation. To identify factors influencing tRNA biogenesis, we previously performed a screen for strains carrying mutations that induce lethality when combined with a sup61-T47:2C allele, encoding a mutant form of . Analyzes of two complementation groups led to the identification of Tan1 as a protein involved in formation of the modified nucleoside N4-acetylcytidine (ac4C) in tRNA and Bud13 as a factor controlling the levels of ac4C by promoting TAN1 pre-mRNA splicing. Here, we describe the remaining complementation groups and show that they include strains with mutations in genes for known tRNA biogenesis factors that modify (DUS2, MOD5 and TRM1), transport (LOS1), or aminoacylate (SES1) . Other strains carried mutations in genes for factors involved in rRNA/mRNA synthesis (RPA49, RRN3 and MOT1) or magnesium uptake (ALR1). We show that mutations in not only DUS2, LOS1 and SES1 but also in RPA49, RRN3 and MOT1 cause a reduction in the levels of the altered . These results indicate that Rpa49, Rrn3 and Mot1 directly or indirectly influence biogenesis.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Identification of factors that promote biogenesis of tRNA_CGA^Ser

Zhou

Byström

et al. 2018

RNA Biology

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The La and related RNA‐binding proteins (LARPs): structures, functions, and evolving perspectives

et al. 2017

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La was first identified as a polypeptide component of ribonucleic protein (RNP) complexes targeted by antibodies in autoimmune patients and is now known to be a eukaryote cell-ubiquitous protein. Structure and function studies have shown that La binds to a common terminal motif, UUU-3’OH, of nascent RNA polymerase III (RNAP III) transcripts and protects them from exonucleolytic decay. For precursor-tRNAs, the most diverse and abundant of these transcripts, La also functions as a RNA chaperone that helps to prevent their misfolding. Related to this, we review evidence that suggests that La and its link to RNAP III were significant in the great expansions of the tRNAomes that occurred in eukaryotes. Four families of La-related proteins (LARPs) emerged during eukaryotic evolution with specialized functions. We provide an overview of the high resolution structural biology of La and LARPs. LARP7 family members most closely resemble La but function with a single RNAP III nuclear transcript, 7SK or telomerase RNA. A cytoplasmic isoform of La protein as well as LARPs 6, 4 and 1 function in mRNA metabolism and translation in distinct but similar ways, sometimes with the poly(A)-binding protein (PABP), and in some cases by direct binding to poly(A)-RNA. New structures of LARP domains, some complexed with RNA, provide novel insights into the functional versatility of these proteins. We also consider LARPs in relation to ancestral La protein and potential retention of links to specific RNA-related pathways. One such link may be tRNA surveillance and codon usage by LARP associated mRNAs.

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The emergent role of mitochondrial RNA modifications in metabolic alterations

et al. 2022

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Mitochondrial epitranscriptomics refers to the modifications occurring in all the different RNA types of mitochondria. Although the number of mitochondrial RNA modifications is less than those in cytoplasm, substantial evidence indicates that they play a critical role in accurate protein synthesis. Recent evidence supported those modifications in mitochondrial RNAs also have crucial implications in mitochondrial-related diseases. In the light of current knowledge about the involvement, the association between mitochondrial RNA modifications and diseases arises from studies focusing on mutations in both mitochondrial and nuclear DNA genes encoding enzymes involved in such modifications. Here, we review the current evidence available for mitochondrial RNA modifications and their role in metabolic disorders, and we also explore the possibility of using them as promising targets for prevention and early detection. Finally, we discuss future directions of mitochondrial epitranscriptomics in these metabolic alterations, and how these RNA modifications may offer a new diagnostic and theragnostic avenue for preventive purposes.

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Dual function of the tRNA(m5U54)methyltransferase in tRNA maturation

Cited by 77 publications

References 39 publications

Identification of factors that promote biogenesis of tRNA_CGA^Ser

Identification of factors that promote biogenesis of tRNA_CGA^Ser

The La and related RNA‐binding proteins (LARPs): structures, functions, and evolving perspectives

The emergent role of mitochondrial RNA modifications in metabolic alterations

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Dual function of the tRNA(m5U54)methyltransferase in tRNA maturation

Cited by 77 publications

References 39 publications

Identification of factors that promote biogenesis of tRNACGASer

Identification of factors that promote biogenesis of tRNACGASer

The La and related RNA‐binding proteins (LARPs): structures, functions, and evolving perspectives

The emergent role of mitochondrial RNA modifications in metabolic alterations

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Product

Resources

About

Identification of factors that promote biogenesis of tRNA_CGA^Ser

Identification of factors that promote biogenesis of tRNA_CGA^Ser