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

FEBS Letters

Kishi, Fumio²  Kotani, Susumu¹  Nakagawa, Hiroyuki¹  Tokuraku, Kiyotaka¹ 

[1] Department of Biochemical Engineering and Science, Faculty of Computer Science and Systems Engineering, Kyushu Institute of Technology, Iizuka, Fukuoka 820-8502, Japan;Center for Gene Research, Yamaguchi University, 1144 Kogushi, Ube, Yamaguchi 755, Japan

关键词: MAP;    Microtubule;    Natural resistance;    NRAMP1;    NRAMP1;    Natural resistance-associated macrophage protein 1;    MAP;    microtubule-associated protein;    GST;    glutathione S-transferase;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;    GST extract;    E. coli crude extracts containing GST;    GST-NRAMP11∼81 extract;    E. coli crude extracts containing GST-NRAMP11∼81;   

DOI  :  10.1016/S0014-5793(98)00488-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown