Med5(Nut1) and Med17(Srb4) are direct targets of mediator histone H4 tail interactions.

Med5(Nut1) and Med17(Srb4) are direct targets of mediator histone H4 tail interactions.
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DOI:
10.1371/journal.pone.0038416
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发表时间:
2012
期刊:
影响因子:
3.7
通讯作者:
Myers LC
Myers LC
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Liu Z;Myers LC

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The Mediator complex transmits activation signals from DNA bound transcription factors to the core transcription machinery. In addition to its canonical role in transcriptional activation, recent studies have demonstrated that S. cerevisiae Mediator can interact directly with nucleosomes, and their histone tails. Mutations in Mediator subunits have shown that Mediator and certain chromatin structures mutually impact each other structurally and functionally in vivo. We have taken a UV photo cross-linking approach to further delineate the molecular basis of Mediator chromatin interactions and help determine whether the impact of certain Mediator mutants on chromatin is direct. Specifically, by using histone tail peptides substituted with an amino acid analog that is a UV activatible crosslinker, we have identified specific subunits within Mediator that participate in histone tail interactions. Using Mediator purified from mutant yeast strains we have evaluated the impact of these subunits on histone tail binding. This analysis has identified the Med5 subunit of Mediator as a target for histone tail interactions and suggests that the previously observed effect of med5 mutations on telomeric heterochromatin and silencing is direct.
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