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@ARTICLE{Yayli:282716,
      author       = {G. Yayli and A. Bernardini and P. K. Mendoza Sanchez$^*$
                      and E. Scheer and M. Damilot and K. Essabri and B. Morlet
                      and L. Negroni and S. D. Vincent and H. T. M. Timmers$^*$
                      and L. Tora},
      title        = {{ATAC} and {SAGA} co-activator complexes utilize
                      co-translational assembly, but their cellular localization
                      properties and functions are distinct.},
      journal      = {Cell reports},
      volume       = {42},
      number       = {9},
      issn         = {2211-1247},
      address      = {[New York, NY]},
      publisher    = {Elsevier},
      reportid     = {DKFZ-2023-01842},
      pages        = {113099},
      year         = {2023},
      abstract     = {To understand the function of multisubunit complexes, it is
                      of key importance to uncover the precise mechanisms that
                      guide their assembly. Nascent proteins can find and bind
                      their interaction partners during their translation, leading
                      to co-translational assembly. Here, we demonstrate that the
                      core modules of ATAC (ADA-two-A-containing) and SAGA
                      (Spt-Ada-Gcn5-acetyltransferase), two lysine acetyl
                      transferase-containing transcription co-activator complexes,
                      assemble co-translationally in the cytoplasm of mammalian
                      cells. In addition, a SAGA complex containing all of its
                      modules forms in the cytoplasm and acetylates non-histone
                      proteins. In contrast, ATAC complex subunits cannot be
                      detected in the cytoplasm of mammalian cells. However, an
                      endogenous ATAC complex containing two functional modules
                      forms and functions in the nucleus. Thus, the two related
                      co-activators, ATAC and SAGA, assemble using
                      co-translational pathways, but their subcellular
                      localization, cytoplasmic abundance, and functions are
                      distinct.},
      keywords     = {CP: Molecular biology (Other) / RIP (Other) / RNA
                      immunoprecipitation (Other) / YEATS2 (Other) / ZZZ3 (Other)
                      / biogenesis (Other) / co-translation (Other) / lysine
                      acetylation (Other) / multiprotein complex (Other) /
                      non-histone protein (Other) / ribosome (Other) /
                      single-molecule RNA FISH (Other) / transcription regulation
                      (Other)},
      cin          = {FR01},
      ddc          = {610},
      cid          = {I:(DE-He78)FR01-20160331},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37682711},
      doi          = {10.1016/j.celrep.2023.113099},
      url          = {https://inrepo02.dkfz.de/record/282716},
}