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Ubiquitin modification of cellular proteins has been shown to be involved with a wide range of biochemical processes including proteasomal degradation, signal transduction, DNA repair, endocytosis and autophagy.
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The Rpt6 tail exhibits a distinct functional relationship with Nas6 in vivo.(a) Phenotypic analysis showing effect of nas6Δ on the growth of rpt6-Δ1 or rpt3-Δ1 single, or double mutants. Four-fold serial dilutions of indicated cells were spotted onto YPD plates, synthetic complete medium (SC), or SC medium containing canavanine (1 μg/ml), and incubated for 2–3 days at the indicated temperature. For testing sensitivity to canavanine (an arginine analog), arginine was omitted from the SC medium. (b) Effect of nas6Δ on the degradation of polyubiquitinated proteins in rpt6-Δ1 or rpt3-Δ1 single, or double mutant cells. The cells were cultured for 6 hours at 37 °C. Whole cell lysates (20 μg) were subjected to 10% Bis-Tris SDS-PAGE for immunoblotting (IB) of polyubiquitinated proteins, and 12% SDS-PAGE for immunoblotting of Nas6 and proteasome subunits. Rpt3 and Rpt6 are base subunits. Rpn8 is a lid subunit. Pgk1 serves as a loading control. Lighter exposure of anti-ubiquitin (Ub) immunoblot is shown at right to further illustrate the difference in polyubiquitinated protein levels. Molecular weight markers are at left in kDa.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Proteasome Activation is Mediated via a Functional Switch of the Rpt6 C-terminal Tail Following Chaperone-dependent Assembly. Sci Rep (2015)
Together, the Rpt3 and Rpt6 tails play a central role in proteasome function.(a) Yeast growth assay showing severe heat sensitivity of rpt3-Δ1rpt6-Δ1 double mutant cells. Four-fold serial dilutions of indicated yeast strains were spotted onto YPD plates and grown for 2–3 days at 30 °C and 37 °C. Table 1 lists the yeast strains used in each figure henceforth. (b) Anti-ubiquitin immunoblots showing an accumulation of polyubiquitinated proteins in rpt3-Δ1rpt6-Δ1 cells. Levels of the Nas6 chaperone and proteasome subunits remained largely unchanged in all indicated strains. Whole cell lysates (20 μg) were subjected to 10% Bis-Tris SDS-PAGE for immunoblotting (IB) of polyubiquitinated proteins, and 12% Tris-Glycine SDS-PAGE (SDS-PAGE henceforth) for immunoblotting of Nas6 and proteasome subunits. Nas6 is a cognate chaperone of Rpt3. Rpt3 and Rpt6 are base subunits. Rpn8 is a lid subunit. Pgk1 serves as a loading control. Ub is ubiquitin. Molecular weight markers are at left in kDa.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Proteasome Activation is Mediated via a Functional Switch of the Rpt6 C-terminal Tail Following Chaperone-dependent Assembly. Sci Rep (2015)
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RUO – Research Use Only |
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