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. 2016 Feb 1;30(3):281–292. doi: 10.1101/gad.274118.115

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© 2016 Coffill et al.; Published by Cold Spring Harbor Laboratory Press

This article, published in Genes & Development, is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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Figure 6. — p53 degradation by Mdm2 is conserved in lampreys. (A) Protein sequence alignment of the RING domain of Mdm2 from lampreys, elephant sharks (Eshark), zebrafish, frogs, chickens, mice, and humans. Accession numbers are in the legend for Figure 3A. The top arrow indicates that all Mdm2 RING domains terminate exactly 13 amino acids residues following the last cysteine. The bottom arrow marks the cysteine residue mutated to generate a nonfunctional Lj-Mdm2 that is unable to degrade Lj-p53. (B) Western blot of Lj-p53 levels following cotransfection with various Lj-Mdm2-expressing constructs. (Lane 1) Lj-p53. (Lane 2) Lj-p53 with MG132. (Lane 3) Lj-p53 + HA-Lj-Mdm2. (Lane 4) Lj-p53 + HA-Lj-Mdm2 with MG132. (Lane 5) Lj-p53 + Lj-Mdm2-HA. (Lane 6) Lj-p53 + Lj-Mdm2-HA with MG132. (Lane 7) Lj-p53 + HA-Lj-Mdm2(C464A). (Lane 8) Lj-p53 + HA-Lj-Mdm2(C464A) with MG132. Lj-Mdm2 levels are shown in the top panel, and the loading control is shown in the bottom panel.