The RNA polymerase III transcription apparatus11Edited by P. E. Wright

Geiduschek, E. Peter; Kassavetis, George A.

doi:10.1006/jmbi.2001.4732

Cited by 347 publications

(334 citation statements)

References 247 publications

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“…RNA Pol III transcribes the 5S rRNA, tRNAs, and other stable noncoding RNAs (Geiduschek and Kassavetis 2001). TORC1 regulates RNA Pol III via its conserved repressor, Maf1 (Upadhya et al 2002).…”

mentioning

confidence: 99%

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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mentioning

confidence: 99%

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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“…However, a number of recently defined factors are now known to be involved (8,9). For Pol III termination in yeast, a critical subunit of the enzyme, Rpc11p, is required for what may be a largely factor-independent process (3,10). In contrast, Pol I termination in yeast has been shown to use a DNA-binding factor, Reb1p, which identifies a well defined sequence element at the 3Ј ends of the primary Pol I transcription unit.…”

mentioning

confidence: 99%

Transcriptional termination by RNA polymerase I requires the small subunit Rpa12p

Prescott

Osheim

Jones

et al. 2004

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

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We identify Rpa12p of RNA polymerase I (Pol I) as a termination factor. Combined analyses using transcription run-on, electron microscopy-visualized chromatin spreading and RT-PCR have been applied to the rRNA-encoding genes of Saccharomyces cerevisiae. These confirm that Pol I termination occurs close to the Reb1p-dependent terminator in wild-type strains. However, deletion mutants for the 3 end-processing enzyme Rnt1p or the Rpa12p subunit of Pol I both show Pol I transcription in the spacer. For ⌬rpa12, these spacer polymerases are devoid of nascent transcripts, suggesting they are immediately degraded. The homology of Rpa12p to the small subunit Rpb9p of Pol II and Rpc11p of Pol III, both implicated in transcriptional termination, points to a common termination mechanism for all three classes of RNA polymerase.

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“…The fragments contained at least 200 bp each upstream and downstream of the endogenous tRNA gene, which included all the regulatory elements necessary for tRNA transcription. 26 , 27 We transfected several tRNA vectors into mammalian cells and confirmed the overexpression of these tRNAs via RT-PCR (Fig. S1A).…”

Section: Resultsmentioning

confidence: 83%

Transfer-RNA-mediated enhancement of ribosomal proteins S6 kinases signaling for cell proliferation

et al. 2018

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While transfer-RNAs (tRNAs) are known to transport amino acids to ribosome, new functions are being unveiled from tRNAs and their fragments beyond protein synthesis. Here we show that phosphorylation of 90-kDa RPS6K (ribosomal proteins S6 kinase) was enhanced by tRNALeu overexpression under amino acids starvation condition. The phosphorylation of 90-kDa RPS6K was decreased by siRNA specific to tRNALeu and was independent to mTOR (mammalian target of rapamycin) signaling. Among the 90-kDa RPS6K family, RSK1 (ribosomal S6 kinase 1) and MSK2 (mitogen-and stress-activated protein kinase 2) were the major kinases phosphorylated by tRNALeu overexpression. Through SILAC (stable isotope labeling by/with amino acids in cell culture) and combined mass spectrometry analysis, we identified EBP1 (ErbB3-binding protein 1) as the tRNALeu-binding protein. We suspected that the overexpression of free tRNALeu would reinforce ErbB2/ErbB3 signaling pathway by disturbing the interaction between ErbB3 and EBP1, resulting in RSK1/MSK2 phosphorylation, improving cell proliferation and resistance to death. Analysis of samples from patients with breast cancer also indicated an association between tRNALeu overexpression and the ErbB2-positive population. Our results suggested a possible link between tRNALeu overexpression and RSK1/MSK2 activation and ErbB2/ErbB3 signaling.

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The RNA polymerase III transcription apparatus11Edited by P. E. Wright

Cited by 347 publications

References 247 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

Transcriptional termination by RNA polymerase I requires the small subunit Rpa12p

Transfer-RNA-mediated enhancement of ribosomal proteins S6 kinases signaling for cell proliferation

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