2016
DOI: 10.1074/jbc.m116.756098
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Role for the MED21-MED7 Hinge in Assembly of the Mediator-RNA Polymerase II Holoenzyme

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Cited by 26 publications
(30 citation statements)
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“…As Δ7ScMed21 did not increase reporter expression when compared to Δ5ScMed21 yet did have a noticeable impact on growth, we did not use it in further analyses. Deletions of ScMed21 Nterminal residues had no effect on repression in SLARC H1-H5 but they do impair auxin responsive transcriptional activation ( Figure 4I), consistent with the role of this region in promoting Pol-II recruitment (Sato et al, 2016). The fully repressed SLARC N188 in Δ3ScMed21 or Δ5ScMed21 mutants showed elevated transcription of the reporter and when depleted demonstrate an increase in reporter activity ( Figure 4J), indicating that there is still residual TPLN188-Mediator interaction taking place.…”
Section: Resultssupporting
confidence: 65%
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“…As Δ7ScMed21 did not increase reporter expression when compared to Δ5ScMed21 yet did have a noticeable impact on growth, we did not use it in further analyses. Deletions of ScMed21 Nterminal residues had no effect on repression in SLARC H1-H5 but they do impair auxin responsive transcriptional activation ( Figure 4I), consistent with the role of this region in promoting Pol-II recruitment (Sato et al, 2016). The fully repressed SLARC N188 in Δ3ScMed21 or Δ5ScMed21 mutants showed elevated transcription of the reporter and when depleted demonstrate an increase in reporter activity ( Figure 4J), indicating that there is still residual TPLN188-Mediator interaction taking place.…”
Section: Resultssupporting
confidence: 65%
“…We observed that the equivalent truncation of AtMED21 (AtMED21-N31) was sufficient for interaction with TPL-N188 ( Figure 2A). We next created truncations of the N-terminal domain of AtMED21 to closely match those that had been made in yeast ( Figure 2B, Supplemental Figure 2B) where deletion of the first five amino acids of ScMed21 (ScΔ5Med21) severely reduce the ability of the Mediator complex to co-purify with Pol-II and CDK8 kinase complex (Sato et al, 2016).…”
Section: Resultsmentioning
confidence: 99%
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“…1, shown as red tail on Pol II) is comprised of numerous repeats of the consensus sequence Y 1 S 2 P 3 T 4-S 5 P 6 S 7 . The Pol II CTD is largely unphosphorylated during initiation, allowing stabilizing interactions of the unmodified CTD with the Mediator complex (Wong et al 2014;Sato et al 2016;Tsai et al 2017). However, across the transcription cycle, the CTD repeats are posttranslationally modified at distinct sites, which stimulates stage-appropriate interactions with transcription initiation, elongation, and RNA processing factors (Buratowski 2009).…”
Section: Pausing Takes Center Stage In Gene Regulationmentioning
confidence: 99%
“…It was previously described that human Rpb3 (hRPB3) binds to transcription factors ATF4 [33] and myogenin [34], and that human Rpb11 (hRPB11a) interacts with Che-1 (AATF) [35]. These interactions lead to transcription activation without significant Mediator involvement [36], because the Mediator also binds the RNA polymerase II on the side of the Rpb3-Rpb11 heterodimer [37][38][39][40].…”
Section: Discussionmentioning
confidence: 99%