ArticleProceedings of the National Academy of Sciences of the United States of America2009
Med8, Med18, and Med20 subunits of the Mediator head domain are interdependent upon each other for folding and complex formation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Non-canonical subunit functions in multiprotein complexes: insights from the Mediator complex.Biochemical Society transactions · 2026Review
- Unique Role of Med8 in Ace2 Recruitment and Target Gene Expression inJournal of microbiology and biotechnology · 2025Article
- Twenty years of Mediator complex structural studies.Biochemical Society transactions · 2019Review
- MEDIATOR18 and MEDIATOR20 confer susceptibility to Fusarium oxysporum in Arabidopsis thaliana.PloS one · 2017Article
- The Mediator complex in plants: structure, phylogeny, and expression profiling of representative genes in a dicot (Arabidopsis) and a monocot (rice) during reproduction and abiotic stress.Plant physiology · 2011Article
- Gene-specific transcription activation via long-range allosteric shape-shifting.The Biochemical journal · 2011Review
- PRIC295, a Nuclear Receptor Coactivator, Identified from PPARα-Interacting Cofactor Complex.PPAR research · 2010Article
Corrections and comments
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Authors and funding
4 authors.
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Abstract
We have studied folding and complex formation of the yeast Mediator head-module protein subunits Med8, Med18, and Med20. Using a combination of immunoprecipitation, far-UV circular dichroism, and fluorescence measurements on recombinantly expressed and denatured proteins that were allowed to renature separately or in different combinations, we found that Med8, Med18, and Med20 can fold in different ways to form both soluble monomeric proteins and different distinct subcomplexes. However, the concurrent presence of all three protein subunits during the renaturation process is required for proper folding and trimer complex formation.
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