THE PARAMYXOVIRUS SV5 V-PROTEIN BINDS 2 ATOMS OF ZINC AND IS A STRUCTURAL COMPONENT OF VIRIONS

被引:124
作者
PATERSON, RG [1 ]
LESER, GP [1 ]
SHAUGHNESSY, MA [1 ]
LAMB, RA [1 ]
机构
[1] NORTHWESTERN UNIV,HOWARD HUGHES MED INST,EVANSTON,IL 60208
关键词
D O I
10.1006/viro.1995.1135
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The paramyxovirus simian virus 5 (SV5) cysteine-rich V protein has been shown to be a virus structural protein by analysis of the polypeptides of purified SV5 virions. In addition, the V protein has been identified as a component of the virus nucleocapsid core both by the analysis of the polypeptides present in radioactively labeled preparations of purified nucleocapsids and by immunoelectron microscopy. Quantitative autoradiography was used to determine that there are similar to 350 molecules of the V protein in virions. The V protein has been purified from V recombinant baculovirus-infected insect cells and by using inductively coupled argon plasma atomic emission spectroscopy it was found that each molecule of V binds two zinc atoms. (C) 1995 Academic Press, Inc.
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页码:121 / 131
页数:11
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