Proteomic Interactome of C. elegans Mediator Complex Subunit 28 (MDT-28) Reveals Predominant Association with a Restricted Set of Core Mediator Subunits and an Affinity to Additional Structural and Enzymatic Proteins
Jazyk angličtina Země Česko Médium print
Typ dokumentu časopisecké články
PubMed
32362303
DOI
10.14712/fb2019065050203
PII: file/5906/fb2019a0021.pdf
Knihovny.cz E-zdroje
- MeSH
- alely MeSH
- Caenorhabditis elegans metabolismus MeSH
- jaderné proteiny metabolismus MeSH
- mediátorový komplex metabolismus MeSH
- podjednotky proteinů metabolismus MeSH
- proteiny Caenorhabditis elegans metabolismus MeSH
- proteomika * MeSH
- vazba proteinů MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- jaderné proteiny MeSH
- MDT-28 protein, C elegans MeSH Prohlížeč
- mediátorový komplex MeSH
- podjednotky proteinů MeSH
- proteiny Caenorhabditis elegans MeSH
Transcription factors exert their regulatory potential on RNA polymerase II machinery through a multiprotein complex called Mediator complex or Mediator. The Mediator complex integrates regulatory signals from cell regulatory cascades with the regulation by transcription factors. The Mediator complex consists of 25 subunits in Saccharomyces cerevisiae and 30 or more subunits in multicellular eukaryotes. Mediator subunit 28 (MED28), along with MED30, MED23, MED25 and MED26, belong to presumably evolutionarily new subunits that seem to be absent in unicellular eukaryotes and are likely to have evolved together with multicellularity and cell differentiation. Previously, we have shown that an originally uncharacterized predicted gene, F28F8.5, is the true MED28 orthologue in Caenorhabditis elegans (mdt-28) and showed that it is involved in a spectrum of developmental processes. Here, we studied the proteomic interactome of MDT-28 edited as GFP::MDT-28 using Crispr/Cas9 technology or MDT-28::GFP expressed from extrachromosomal arrays in transgenic C. elegans exploiting the GFPTRAP system and mass spectrometry. The results show that MDT-28 associates with the Head module subunits MDT-6, MDT-8, MDT-11, MDT-17, MDT- 20, MDT-22, and MDT-30 and the Middle module subunit MDT-14. The analyses also identified additional proteins as preferential MDT-28 interactants, including chromatin-organizing proteins, structural proteins and enzymes. The results provide evidence for MDT-28 engagement in the Mediator Head module and support the possibility of physical (direct or indirect) interaction of MDT-28 with additional proteins, reflecting the transcription-regulating potential of primarily structural and enzymatic proteins at the level of the Mediator complex.
Biocev 1st Faculty of Medicine Charles University Vestec Czech Republic
Department of Pathology 3rd Faculty of Medicine Charles University Prague Czech Republic
Laboratory of Mass Spectrometry Faculty of Science Charles University Vestec Czech Republic
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