Not5-dependent co-translational assembly of Ada2 and Spt20 is essential for functional integrity of SAGA | Zendy

Sari Kassem | Zendy; Zoltán Villányi | Zendy; Martine A. Collart | Zendy

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Not5-dependent co-translational assembly of Ada2 and Spt20 is essential for functional integrity of SAGA

Author(s) -

Sari Kassem,

Zoltán Villányi,

Martine A. Collart

Publication year - 2016

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/gkw1059

Subject(s) - biology , acetylation , protein subunit , histone , saccharomyces cerevisiae , chaperone (clinical) , acetyltransferase , microbiology and biotechnology , genetics , gene , biochemistry , medicine , pathology

Acetylation of histones regulates gene expression in eukaryotes. In the yeast Saccharomyces cerevisiae it depends mainly upon the ADA and SAGA histone acetyltransferase complexes for which Gcn5 is the catalytic subunit. Previous screens have determined that global acetylation is reduced in cells lacking subunits of the Ccr4–Not complex, a global regulator of eukaryotic gene expression. In this study we have characterized the functional connection between the Ccr4–Not complex and SAGA. We show that SAGA mRNAs encoding a core set of SAGA subunits are tethered together for co-translational assembly of the encoded proteins. Ccr4–Not subunits bind SAGA mRNAs and promote the co-translational assembly of these subunits. This is needed for integrity of SAGA. In addition, we determine that a glycolytic enzyme, the glyceraldehyde-3-phosphate dehydrogenase Tdh3, a prototypical moonlighting protein, is tethered at this site of Ccr4–Not-dependent co-translational SAGA assembly and functions as a chaperone.

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