Journal of Proteomics & Bioinformatics
Open Access

Matthew D.Galbraith

Publications

• Research Article
  Mutual Exclusivity of MED12/MED12L, MED13/13L, and CDK8/19 Paralogs Revealed within the CDK-Mediator Kinase Module
  Author(s): Danette L. Daniels, Michael Ford, Marie K. Schwinn, Hélène Benink, Matthew D.Galbraith, Ravi Amunugama, Richard Jones, DavidAllen, NorikoOkazaki, Hisashi Yamakawa, Futaba Miki, Takahiro Nagase, Joaquín M.Espinosa and Marjeta UrhDanette L. Daniels, Michael Ford, Marie K. Schwinn, Hélène Benink, Matthew D.Galbraith, Ravi Amunugama, Richard Jones, DavidAllen, NorikoOkazaki, Hisashi Yamakawa, Futaba Miki, Takahiro Nagase, Joaquín M.Espinosa and Marjeta Urh
  
  The macromolecular complex Mediator plays important roles in regulation of RNA Polymerase II (RNAPII) activity by DNA-binding proteins, non-coding RNAs, and chromatin. Structural and biochemical studies have shown that human Mediator exists in two forms; a core complex of 26 proteins, termed Mediator, and a larger complex containing the CDK8 kinase module, termed CDK8-Mediator. Interestingly, 3 subunits of the kinase module have undergone independent gene duplications in vertebrates to generate the paralog pairs MED12/MED12L, MED13/ MED13L, and CDK8/CDK19. Each has been shown to interact with Mediator, yet clearly defining the composition of CDK kinase module has been challenging due to the large size (~600 kD), the similarities between paralogs, and potential combinatorial nature of complexes. In this study, we performed a systematic proteomic analysis using HaloTag technology t.. View More»
  DOI: 10.4172/jpb.S2-004

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