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TcPINK1 autophosphorylates and phosphorylates PINKtide.

By Liesbeth Aerts (846710), Katleen Craessaerts (846711), Bart De Strooper (189361) and Vanessa A. Morais (189353)

Abstract

<p>(A) Purity of <i>E</i>. <i>coli</i>-expressed WT and KI TcPINK1 was evaluated by Coomassie staining. Both forms of TcPINK1 are equally enriched. (B) Quantification of [γ-32P]-ATP <i>in vitro</i> autophosphorylation of purified WT or KI TcPINK1. (C) Quantification of [γ-32P]-ATP <i>in vitro</i> phosphorylation of PINKtide by purified WT or KI TcPINK1 (mean ± SEM, n = 4 independent experiments). Statistical significance was calculated between WT and KI TcPINK1 using Student’s <i>t</i>-test (*: p-value < 0.05; **: p-value < 0.01).</p

Topics: Uncategorised, Histone H 1, Triboleum castaneum PINK 1, Triboleum castaneum PINK 1 Orthologues Mutations, PINK 1., substrate, PINK 1 phosphorylate Parkin, PINK 1 orthologues, Triboleum castaneum PINK 1 insect orthologue
Year: 2016
DOI identifier: 10.1371/journal.pone.0146083.g002
OAI identifier: oai:figshare.com:article/1639340
Provided by: FigShare
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