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Human natural resistance‐associated macrophage protein is a new type of microtubule‐associated protein
Author(s) -
Tokuraku Kiyotaka,
Nakagawa Hiroyuki,
Kishi Fumio,
Kotani Susumu
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00488-8
Subject(s) - microtubule , fusion protein , microtubule associated protein , microbiology and biotechnology , biology , chemistry , biochemistry , recombinant dna , gene
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 NH 2 ‐terminal domain to bind to taxol‐stabilized microtubules. Co‐sedimentation analysis showed that the fusion protein binds to microtubules. Although the NH 2 ‐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.