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. Author manuscript; available in PMC: 2019 Dec 20.
Published in final edited form as: Mol Cell. 2018 Nov 8;72(6):985–998.e7. doi: 10.1016/j.molcel.2018.10.007

Figure 4: PACS2 and DBC1 synergistically inhibit SIRT1 activity in vitro.

Figure 4:

(A) Top: Superposition of 1H-15N HSQC spectra of 30 µM DBC1 S1-L alone (black) or in the presence of 70 µM full-length human SIRT1 (green). Middle: Superposition of 1H-15N HSQC spectra of 30 µM DBC1 S1-L alone (black) or in the presence of 70 µM human SIRT1 Δ6-83 (green). Bottom: Superposition of 1H-15N HSQC spectra of 30 µM DBC1 S1-L alone (black) or in the presence of 70 µM PACS-2 FBR (red). Ellipses highlight a region in the DBC1 S1-L spectrum where peak broadening and dramatic chemical shift changes in the presence of SIRT1 (top panel) but not SIRT1 Δ6-83 or PACS-2 FBR (middle and bottom panels, respectively) occur. (B) Enzyme assay using the Ac-Lys778-PGC-1α peptidyl substrate of recombinant human SIRT1, SIRT1 Δ6-83 or SIRT1S162D with the indicated combinations of recombinant DBC1 S1-L and PACS-2 FBR. Enzyme reactions were conducted as described in Methods.