Human natural resistance-associated macrophage protein is a new type of microtubule-associated protein

FEBS Lett. 1998 May 22;428(1-2):63-7. doi: 10.1016/s0014-5793(98)00488-8.

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