Abstract
Natural resistance-associated macrophage protein 1 (NRAMP1) is a putative membrane protein that dominates natural resistance to infection. An NRAMP1-glutathione S-transferase fusion protein was used to test the ability of the NRAMP1 NH2-terminal domain to bind to taxol-stabilized microtubules. Co-sedimentation analysis showed that the fusion protein binds to microtubules. Although the NH2-terminal domain of the NRAMP1 molecule has structural homology with the Pro-rich region of microtubule-associated protein 4 (MAP4), the presence of the MAP4 microtubule-binding domain fragment had little effect on the binding of the fusion protein to microtubules.
MeSH terms
-
Animals
-
Binding Sites
-
Binding, Competitive
-
Carrier Proteins / genetics
-
Carrier Proteins / isolation & purification
-
Carrier Proteins / metabolism*
-
Cation Transport Proteins*
-
Cattle
-
Glutathione Transferase / genetics
-
Glutathione Transferase / metabolism
-
Humans
-
Immunity, Innate*
-
Macrophages / metabolism*
-
Membrane Proteins / genetics
-
Membrane Proteins / isolation & purification
-
Membrane Proteins / metabolism*
-
Microtubule-Associated Proteins / genetics
-
Microtubule-Associated Proteins / isolation & purification
-
Microtubule-Associated Proteins / metabolism*
-
Paclitaxel / pharmacology
-
Recombinant Fusion Proteins / genetics
-
Recombinant Fusion Proteins / isolation & purification
-
Recombinant Fusion Proteins / metabolism
Substances
-
Carrier Proteins
-
Cation Transport Proteins
-
Membrane Proteins
-
Microtubule-Associated Proteins
-
Recombinant Fusion Proteins
-
natural resistance-associated macrophage protein 1
-
Glutathione Transferase
-
Paclitaxel