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USP7-CTD interacts with GMPS and UHRF1 peptides.

By Roland Pfoh (750449), Ira Kay Lacdao (750450), Anna A. Georges (750451), Adam Capar (750452), Hong Zheng (151877), Lori Frappier (87668) and Vivian Saridakis (750453)

Abstract

<p>(A) Alignment and dissociation constants of ICP0, GMPS and UHRF1 peptides. (B) Location of the KxxxK motif (<sup>316</sup>DRTPRKRISKTLN<sup>328</sup>) within a disordered loop on the GMPS crystal structure (PDB ID 2VXO). (C) Coomassie stained gel of GST pull-down assays with WT or mutant USP7-CTD (D762A, D764A and D762A/D764A) and GST-GMPS peptide. Lane 1 USP7-CTD and GST-GMPS peptide load, lanes 2–5 are the eluted fractions with WT and mutant USP7-CTD. (D) Coomassie stained gel of GST pull-down assays with WT USP7-CTD and mutant GST-GMPS peptides. Lanes 1 (load) and 2 (elute) USP7-CTD and WT GST-GMPS, lanes 3–5 are the eluted fractions with GST-GMPS mutants (K321A, K325A and K321A/K325A). (E) Coomassie stained gel of GST pull-down assays with WT or mutant USP7-CTD (D762A, D762A/D764A and D762R/D764R) and GST-UHRF1 peptide. Lanes 1–4 are the loaded fractions with WT and mutant USP7-CTD. Lanes 5–8 are the eluted fractions with WT and mutant USP7-CTD. (F) Coomassie stained gel of GST pull-down assays with WT USP7-CTD and mutant GST-UHRF1 peptides. Lanes 1–4 are the loaded fractions with WT and mutant (K644A, K648A and K644A/K648A) GST-UHRF1. Lanes 5–8 are the eluted fractions with WT and mutant (K644A, K648A and K644A/K648A) GST-UHRF1. In all instances, approximately 1–2% of the input and 2.5% of the eluate is loaded on the gels.</p

Topics: Biological Sciences, USP 7 recognition, Ubl 2 binding pocket, Target USP 7 Herpes simplex virus, gmps, ICP 0 peptide, ICP 0, UHRF, 26 S proteasomal, USP 7 regulation, ctd, Ubl 2 mutation, Several USP 7 partners, deubiquitinating enzyme USP 7, USP 7, Ubl 2. Sequences
Year: 2015
DOI identifier: 10.1371/journal.ppat.1004950.g004
OAI identifier: oai:figshare.com:article/1438967
Provided by: FigShare
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