Mutation in a new gene MAF1 affects tRNA suppressor efficiency in Saccharomyces cerevisiae

Boguta, Magdalena; Czerska, Kamila; Żołądek, Teresa

doi:10.1016/s0378-1119(96)00669-5

Cited by 74 publications

(70 citation statements)

References 18 publications

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“…4E). This result fits with the previously proposed model that accumulation of tRNA in maf1 cells is detrimental to mitochondrial function (Boguta et al 1997). …”

Section: Torc1 Regulates Rna Pol III Through Sch9supporting

confidence: 92%

Characterization of the rapamycin-sensitive phosphoproteome reveals that Sch9 is a central coordinator of protein synthesis

Huber¹,

Bodenmiller²,

Uotila³

et al. 2009

Genes Dev.

316

404

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The target of rapamycin complex 1 (TORC1) is an essential multiprotein complex conserved from yeast to humans. Under favorable growth conditions, and in the absence of the macrolide rapamycin, TORC1 is active, and influences virtually all aspects of cell growth. Although two direct effectors of yeast TORC1 have been reported (Tap42, a regulator of PP2A phosphatases and Sch9, an AGC family kinase), the signaling pathways that couple TORC1 to its distal effectors were not well understood. To elucidate these pathways we developed and employed a quantitative, label-free mass spectrometry approach. Analyses of the rapamycin-sensitive phosphoproteomes in various genetic backgrounds revealed both documented and novel TORC1 effectors and allowed us to partition phosphorylation events between Tap42 and Sch9. Follow-up detailed characterization shows that Sch9 regulates RNA polymerases I and III, the latter via Maf1, in addition to translation initiation and the expression of ribosomal protein and ribosome biogenesis genes. This demonstrates that Sch9 is a master regulator of protein synthesis.[Keywords: Maf1; Sch9; TOR; phosphoproteomics; rapamycin; ribosome biogenesis] Supplemental material is available at http://www.genesdev.org.

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“…4E). This result fits with the previously proposed model that accumulation of tRNA in maf1 cells is detrimental to mitochondrial function (Boguta et al 1997). …”

Section: Torc1 Regulates Rna Pol III Through Sch9supporting

confidence: 92%

Characterization of the rapamycin-sensitive phosphoproteome reveals that Sch9 is a central coordinator of protein synthesis

Huber¹,

Bodenmiller²,

Uotila³

et al. 2009

Genes Dev.

316

404

View full text Add to dashboard Cite

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“…Overexpression of a 59-terminal fragment as well as point mutations in the RPC160 gene were identified previously as suppressors of the maf1D growth phenotype. That suppression was accompanied by reduction of tRNA levels in maf1D cells (Boguta et al 1997;Pluta et al 2001). In view of those earlier data, the similar suppressor actions of Maf1 and the N-terminal part of Rpc160 on the trm4Dtrm8D growth defect were expected.…”

Section: Discussionsupporting

confidence: 67%

Maf1-mediated repression of RNA polymerase III transcription inhibits tRNA degradation via RTD pathway

Turowski

Karkusiewicz

Kowal

et al. 2012

RNA

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tRNA precursors, which are transcribed by RNA polymerase III, undergo end-maturation, splicing, and base modifications. Hypomodified tRNAs, such as tRNA Val(AAC) , lacking 7-methylguanosine and 5-methylcytidine modifications, are subject to degradation by a rapid tRNA decay pathway. Here we searched for genes which, when overexpressed, restored stability of tRNA Val(AAC) molecules in a modification-deficient trm4Dtrm8D mutant. We identified TEF1 and VAS1, encoding elongation factor eEF1A and valyl-tRNA synthetase respectively, which likely protect hypomodified tRNA Val(AAC) by direct interactions. We also identified MAF1 whose product is a general negative regulator of RNA polymerase III. Expression of a Maf1-7A mutant that constitutively repressed RNA polymerase III transcription resulted in increased stability of hypomodified tRNA Val(AAC) . Strikingly, inhibition of tRNA transcription in a Maf1-independent manner, either by point mutation in RNA polymerase III subunit Rpc128 or decreased expression of Rpc17 subunit, also suppressed the turnover of the hypomodified tRNA Val(AAC) . These results support a model where inhibition of tRNA transcription leads to stabilization of hypomodified tRNA Val(AAC) due to more efficient protection by tRNA-interacting proteins.

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“…tRNA modifying enzyme (12,13,19), we also tested mod5Δ and found that it alleviates tgm silencing (Fig. 1B) and has no negative growth phenotype under normal conditions.…”

Section: Significancementioning

confidence: 97%

“…Mod5 was originally tested for tgm silencing effects because of its genetic interaction with Maf1 (12,13). Even so, it was not entirely expected that Mod5 would affect tgm silencing, because its previously known function is the isopentenylation of the A37 exocyclic amine in the tRNAs tRNA Tyr , tRNA Phe , and tRNA Ser (14)(15)(16)(17).…”

Section: Rna Silencing | Maf1mentioning

confidence: 99%

Mod5 protein binds to tRNA gene complexes and affects local transcriptional silencing

Pratt-Hyatt

Pai²,

Haeusler³

et al. 2013

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

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Significance This study provides new insight into the requirements for observed silencing of RNA polymerase II transcription near tRNA genes. Mod5 is a conserved tRNA modification enzyme found in both the nucleus and cytoplasm, although it only modifies tRNAs in the cytoplasm. Mod5 is required for silencing near tRNA genes, and it is bound to both nuclear tRNA gene complexes and nuclear pre-tRNA transcripts. Possible mechanisms for this form of RNA-mediated transcriptional silencing are discussed.

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Mutation in a new gene MAF1 affects tRNA suppressor efficiency in Saccharomyces cerevisiae

Cited by 74 publications

References 18 publications

Characterization of the rapamycin-sensitive phosphoproteome reveals that Sch9 is a central coordinator of protein synthesis

Characterization of the rapamycin-sensitive phosphoproteome reveals that Sch9 is a central coordinator of protein synthesis

Maf1-mediated repression of RNA polymerase III transcription inhibits tRNA degradation via RTD pathway

Mod5 protein binds to tRNA gene complexes and affects local transcriptional silencing

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