Deubiquitination of H2B by the SAGA complex destabilizes H2B.

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Deubiquitination of H2B by the SAGA complex destabilizes H2B. Deubiquitination of H2B by the SAGA complex destabilizes H2B. (A) Extragenic suppressors of htb1-G52D, identified by suppressor screening followed by mixture sequencing. All suppressors were mapped to SAGA complex genes. (B) and (C) htb1-G52D was crossed with Δubp8 and Δgcn5 to produce double mutants. Spot test results indicated that htb1-G52D was rescued by Δubp8 and Δgcn5. (D) Almost all htb1-G52D single-amino acid-substitution suppressors in Ubp8 were located in the two conserved domains: the ZnF-UBP Domain (ubiquitin-binding domain) and the ubiquitin-specific protease domain, both of which are required for the deubiquitination activity of the SAGA complex. (E) Alignment of Sgf11 among various species and localization of the two htb1-G52D suppressors in Sgf11. Sgf11 binds the H2A/H2B heterodimer via its zinc-finger domain (ZnF domain, the positions of the zinc-coordinating residues are indicated by asterisks). The two Sgf11 point mutations (Q64Stop and C77Y) are mapped to its ZnF domain; therefore, they may decrease H2B deubiquitination by the SAGA complex. (F) Immunoblot patterns using a polyclonal antibody against histone H2B (anti-H2B). Wild type, htb1-G52D, htb1-G52D Δubp8, htb1-G52D Δgcn5, Δubp8, and Δgcn5 were cultured first at 26°, and then shifted to 36° for 5 hr. The upper band is mono-ubiquitinated H2B (uH2B) and the lower band is H2B. Xingya Xu et al. G3 2018;8:1031-1038 ©2018 by Genetics Society of America