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Model of the Mediator middle module based on protein cross-linking
Author(s) -
Laurent Larivière,
Clemens Plaschka,
Martin Seizl,
Evgeniy V. Petrotchenko,
Larissa Wenzeck,
Christoph H. Borchers,
Patrick Cramer
Publication year - 2013
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/gkt704
Subject(s) - biology , tetramer , mediator , protein subunit , computational biology , transcription (linguistics) , rna polymerase ii , homology (biology) , microbiology and biotechnology , genetics , biochemistry , amino acid , gene , gene expression , promoter , linguistics , philosophy , enzyme
The essential core of the transcription coactivator Mediator consists of two conserved multiprotein modules, the head and middle modules. Whereas the structure of the head module is known, the structure of the middle module is lacking. Here we report a 3D model of a 6-subunit Mediator middle module. The model was obtained by arranging crystal structures and homology models of parts of the module based on lysine-lysine cross-links obtained by mass spectrometric analysis. The model contains a central tetramer formed by the heterodimers Med4/Med9 and Med7/Med21. The Med7/Med21 heterodimer is flanked by subunits Med10 and Med31. The model is highly extended, suggests that the middle module is flexible and contributes to a molecular basis for detailed structure-function studies of RNA polymerase II regulation.

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