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Subcellular localization of adenylate kinases in Plasmodium falciparum |
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| Authors: | Jipeng Ma Stefan Rahlfs Esther Jortzik R Heiner Schirmer Jude M Przyborski Katja Becker |
| Institution: | a Biochemistry and Molecular Biology, Interdisciplinary Research Center, Justus Liebig University Giessen, 35392 Giessen, Germany b Biochemistry Center, Heidelberg University, 69120 Heidelberg, Germany c Department of Parasitology, Marburg University, 35043 Marburg, Germany |
| 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.Structured summary of protein interactionsEXP-1 and PfAK2colocalize by fluorescence microscopy (View interaction)PfAK2 and SERPcolocalize by fluorescence microscopy (View interaction) |
| Keywords: | aa amino acid AK adenylate kinase AKLP1 adenylate kinase-like protein 1 AKLP2 adenylate kinase-like protein 2 AP5A P1 P5-di (adenosine-5&prime ) pentaphosphate CRT chloroquine resistance transporter E coli Escherichia coli GAK GTP:AMP phosphotransferase GP5A P1 P5-di (guanosine-5&prime ) pentaphosphate hCINAP human coilin interacting nuclear ATPase protein IRBC infected red blood cell NCBI National Center for Biotechnology Information Ni-NTA nickel-nitrilotriacetate P-loop phosphate binding loop with the canonic sequence GxxGxGxxT PVM parasitophorous vacuole membrane SERP serine-rich protein TBST Tris-buffered saline Tween-20 |
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