SPECIFIC RNA-BINDING BY AMINO-TERMINAL PEPTIDES OF ALFALFA MOSAIC-VIRUS COAT PROTEIN

被引:77
作者
BAER, ML
HOUSER, F
LOESCHFRIES, LS
GEHRKE, L
机构
[1] MIT,DIV HLTH SCI & TECHNOL,BLDG E25-545,CAMBRIDGE,MA 02139
[2] HARVARD UNIV,SCH MED,PROGRAM CELL & DEV BIOL,BOSTON,MA 02115
[3] PURDUE UNIV,DEPT BOT PLANT PATHOL,W LAFAYETTE,IN 47906
关键词
CONFORMATION; PEPTIDE; REPLICATION; RNA PROTEIN INTERACTIONS; VIRUS;
D O I
10.1002/j.1460-2075.1994.tb06312.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Specific RNA - protein interactions and ribonucleoprotein complexes are essential for many biological processes, but our understanding of how ribonucleoprotein particles form and accomplish their biological functions is rudimentary. This paper describes the interaction of alfalfa mosaic virus (AlMV) coat protein or peptides with viral RNA. AlMV coat protein is necessary both for virus particle formation and for the initiation of replication of the three genomic RNAs. We have examined protein determinants required for specific RNA binding and analyzed potential structural changes elicited by complex formation. The results indicate that the amino-terminus of the viral coat protein, which lacks primary sequence homology with recognized RNA binding motifs, is both necessary and sufficient for binding to RNA. Circular dichroism spectra and electrophoretic mobility shift experiments suggest that the RNA conformation is altered when amino-terminal coat protein peptides bind to the viral RNA. The peptide-RNA interaction is functionally significant because the peptides wilt substitute for AlMV coat protein in initiating RNA replication. The apparent conformational change that accompanies RNA - peptide complex formation may generate a structure which, unlike the viral RNA alone, can be recognized by the viral replicase.
引用
收藏
页码:727 / 735
页数:9
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