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The hRpn2-derived peptide depletes hRpn13 from the proteasome.

By Xiuxiu Lu (211648), Fen Liu (317808), Sarah E. Durham (813071), Sergey G. Tarasov (813072) and Kylie J. Walters (23009)

Abstract

<p>(A) 293T cells were transfected with p3XFLAG-CMV7.1-hRpn2 (916–953) WT or F948Stop plasmids and the cell lysates immunoprecipitated with anti-hRpt3 antibodies and immunoprobed with antibodies against hRpn13, hRpt3, and hRpn2, as indicated. (B) Cell lysates from 293T cells transfected with HA-ubiquitin alone or together with either p3XFLAG-CMV7.1-hRpn2 (916–953) WT or F948Stop plasmids were immunoblotted with anti-ubiquitin and anti-β-actin antibodies, as indicated. (C) A model illustrating hRpn2 (916–953) peptide interacting with hRpn13 and displacing it from the proteasome.</p

Topics: Uncategorised, 293 T cells, proteasome ubiquitin receptor, hRpn 2 fragment, pc, er, Displaces Human Rpn 13, domain recruits deubiquitinating enzyme Uch 37, nmr, DEUBAD, cancer cell lines, peptide, 293 T Cells Rpn 13, hRpn 13 Pru domain, Rpn 13 C 88, 12 nM affinity, target hRpn 13 function, hRpn 13
Year: 2015
DOI identifier: 10.1371/journal.pone.0140518.g006
OAI identifier: oai:figshare.com:article/1574407
Provided by: FigShare
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