期刊
PROTEIN EXPRESSION AND PURIFICATION
卷 92, 期 1, 页码 94-99出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pep.2013.09.003
关键词
Matrix protein; Mouse mammary tumor virus; Murine leukemia virus; Myristoylation; N-myristoyltransferase; Retrovirus
类别
资金
- Grant agency of the Czech Republic [204/09/1388]
- OPPK project [CZ.2.16/3.1.00/24016]
- [RVO 61388963]
N-terminal myristoylation of retroviral matrix proteins is essential for the targeting of the Gag polyproteins to the plasma membrane. To investigate the effect of the myristoylation on the structure and membrane binding ability of the matrix proteins, it is necessary to prepare their myristoylated forms. We present purification of myristoylated matrix proteins of the mouse mammary tumor virus and murine leukemia virus, two morphogenetically distinct retroviruses. The proteins were expressed in Escherichia coli coexpressing a yeast N-myristoyltransferase. This E. coli expression system yielded a mixture of myristoylated and nonmyristoylated matrix proteins. We established efficient one-step metal affinity purification that enabled to obtain pure myristoylated matrix proteins suitable for structural and functional studies. (C) 2013 Elsevier Inc. All rights reserved.
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