Journalartikel

Jahr der Veröffentlichung: 2012

Seiten: 3037-3043

Zeitschrift: FEBS Letters

Bandnummer: 586

Heftnummer: 19

ISSN: 0014-5793

Open Access Status: Bronze

DOI Link: https://doi.org/10.1016/j.febslet.2012.07.013

Verlag: Wiley

Abstract: 
Adenylate kinases (AK) play a key role in nucleotide signaling processes and energy metabolism by catalyzing the reversible conversion of ATP and AMP to 2 ADP. In the malaria parasite Plasmodium falciparum this reaction is mediated by AK1, AK2, and a GTP:AMP phosphotransferase (GAK). Here, we describe two additional adenylate kinase-like proteins: PfAKLP1, which is homologous to human AK6, and PfAKLP2. Using GFP-fusion proteins and life cell imaging, we demonstrate a cytosolic localization for PfAK1, PfAKLP1, and PfAXLP2, whereas PfGAK is located in the mitochondrion. PfAK2 is located at the parasitophorous vacuole membrane, and this localization is driven by N-myristoylation.Structured summary of protein interactions:EXP-1 and PfAK2 colocalize by fluorescence microscopy (View interaction)PfAK2 and SERP colocalize by fluorescence microscopy (View interaction) (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Harvard-Zitierstil: Ma, J., Rahlfs, S., Jortzik, E., Schirmer, R., Przyborski, J. and Becker, K. (2012) Subcellular localization of adenylate kinases in Plasmodium falciparum, FEBS Letters, 586(19), pp. 3037-3043. https://doi.org/10.1016/j.febslet.2012.07.013

APA-Zitierstil: Ma, J., Rahlfs, S., Jortzik, E., Schirmer, R., Przyborski, J., & Becker, K. (2012). Subcellular localization of adenylate kinases in Plasmodium falciparum. FEBS Letters. 586(19), 3037-3043. https://doi.org/10.1016/j.febslet.2012.07.013