| Literature DB >> 22819813 |
Jipeng Ma1, Stefan Rahlfs, Esther Jortzik, R Heiner Schirmer, Jude M Przyborski, Katja Becker.
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 PfAKLP2, whereas PfGAK is located in the mitochondrion. PfAK2 is located at the parasitophorous vacuole membrane, and this localization is driven by N-myristoylation.Entities:
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Year: 2012 PMID: 22819813 DOI: 10.1016/j.febslet.2012.07.013
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124