STRUCTURE OF INFLUENZA-VIRUS RNP .1. INFLUENZA-VIRUS NUCLEOPROTEIN MELTS SECONDARY STRUCTURE IN PANHANDLE RNA AND EXPOSES THE BASES TO THE SOLVENT

被引:206
作者
BAUDIN, F
BACH, C
CUSACK, S
RUIGROK, RWH
机构
[1] ILL GRENOBLE,EUROPEAN MOLEC BIOL LAB,GRENOBLE OUTSTN,F-38042 GRENOBLE,FRANCE
[2] UNIV GIESSEN,INST VIROL,D-35392 GIESSEN,GERMANY
关键词
INFLUENZA NUCLEOPROTEIN; REPLICATION; RNA-PROTEIN INTERACTION; RNP; TRANSCRIPTION;
D O I
10.1002/j.1460-2075.1994.tb06614.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
The influenza virus genome consists of eight segments of negative-sense RNA, i.e. the viral (v) RNA forms the template for the mRNA. Each segment is encapsidated by the viral nucleoprotein to form a ribonucleoprotein (RNP) particle and each RNP carries its own polymerase complex. We studied the interaction of purified nucleoprotein with RNA in vitro, by using a variety of enzymatic and chemical probes for RNA conformation. Our results suggest that the nucleoprotein binds to the vRNA backbone without apparent sequence specificity, exposing the bases to the outside and melting all secondary structure. In this way, the viral polymerase may transcribe the RNA without the need for dissociating the nucleoprotein and without being stopped by RNA secondary structure, and the viral RNPs are ready to start transcription as soon as they enter the host cell.
引用
收藏
页码:3158 / 3165
页数:8
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