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.
Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenylate Kinase / genetics
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Adenylate Kinase / metabolism*
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Amino Acid Sequence
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Amino Acid Substitution
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Animals
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Base Sequence
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Cytosol / enzymology
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DNA Primers / genetics
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DNA, Protozoan / genetics
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Humans
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Intracellular Membranes / enzymology
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Mitochondria / enzymology
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Nucleoside-Phosphate Kinase / genetics
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Nucleoside-Phosphate Kinase / metabolism
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Plasmodium falciparum / enzymology*
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Plasmodium falciparum / genetics
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Protozoan Proteins / genetics
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Protozoan Proteins / metabolism*
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Sequence Homology, Amino Acid
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Vacuoles / enzymology
Substances
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DNA Primers
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DNA, Protozoan
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Protozoan Proteins
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Recombinant Fusion Proteins
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nucleoside triphosphate-adenylate kinase
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Adenylate Kinase
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adenylate kinase 1
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adenylate kinase 2
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Nucleoside-Phosphate Kinase