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Chaperonin CCT Checkpoint Function in Basal Transcription Factor TFIID Assembly

Research output: Contribution to journalArticle

Original languageEnglish
Pages (from-to)1119-1127
Number of pages9
JournalNature Structural and Molecular Biology
Volume25
Issue number12
Early online date3 Dec 2018
DOIs
DateAccepted/In press - 25 Oct 2018
DateE-pub ahead of print - 3 Dec 2018
DatePublished (current) - Dec 2018

Abstract

TFIID is a cornerstone of eukaryotic gene regulation. Distinct TFIID complexes with unique subunit composition exist and several TFIID subunits are shared with other complexes, conveying intricate cellular decision making to control subunit allocation and functional assembly of this essential transcription factor. However, the underlying molecular mechanisms remain poorly understood. Here, we used quantitative proteomics to examine TFIID submodules and assembly mechanisms in human cells. Structural and mutational analysis of the cytoplasmic TAF5-TAF6-TAF9 submodule identified novel interactions crucial for TFIID integrity, and for allocating TAF9 to TFIID or the SAGA co-activator complex. We discover a key checkpoint function for the chaperonin CCT, which specifically associates with nascent TAF5 for subsequent handover to TAF6-TAF9 and ultimate holo-TFIID formation. Our findings illustrate at the molecular level how multisubunit complexes are crafted in the cell, involving checkpoint decisions facilitated by a chaperone machine.

    Structured keywords

  • Bristol BioDesign Institute
  • BrisSynBio

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  • Full-text PDF (accepted author manuscript)

    Rights statement: This is the author accepted manuscript (AAM). The final published version (version of record) is available online via Springer Nature at https://www.nature.com/articles/s41594-018-0156-z . Please refer to any applicable terms of use of the publisher.

    Accepted author manuscript, 443 KB, PDF document

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