AN AMINO-PROXIMAL DOMAIN OF THE L-PROTEIN BINDS TO THE P-PROTEIN IN THE MEASLES-VIRUS RNA-POLYMERASE COMPLEX

被引:58
作者
HORIKAMI, SM
SMALLWOOD, S
BANKAMP, B
MOYER, SA
机构
[1] UNIV FLORIDA,COLL MED,DEPT IMMUNOL & MED MICROBIOL,GAINESVILLE,FL 32610
[2] UNIV FLORIDA,COLL MED,DEPT PEDIAT,GAINESVILLE,FL 32610
关键词
D O I
10.1006/viro.1994.1676
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The RNA polymerase of measles virus consists of two virus-encoded subunits, the L and P proteins with 2183 and 507 amino acids, respectively. When these proteins were coexpressed from plasmids in a mammalian expression system, a complex was formed as detected by the coimmunoprecipitation of the L protein with the P protein by anti-P antibodies. Pulse-chase experiments showed that complex formation increased the stability of the L protein. We have used the coimmunoprecipitation assay in conjunction with a series of C-terminal truncations of the L protein to map the region of the L protein which is involved in complex formation with the P protein. Mutant L proteins consisting of the N-terminal 1139, 916, 611, and 408 amino acids all bound to the P protein. An L protein truncation consisting of only the N-terminal 292 amino acids, which deleted part of the conserved domain I, however, did not bind the P protein. The data show that the N-terminal 408 amino acids of the L protein contain the P binding domain and suggest that domain I within this region of the L proteins of (-) strand RNA viruses may be important for RNA polymerase complex formation. (C) 1994 Academic Press, Inc.
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页码:540 / 545
页数:6
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