Translational in vitro activity of the 3a gene and the coat protein gene derived from brome mosaic virus RNA 3 by site‐specific cleavage with RNase H

FEBS Letters

Miroshnichenko, N.A.²  Karpova, O.V.¹  Atabekov, J.G.¹  Smirnyagina, E.V.¹  Rodionova, N.P.¹ 

[1] Department of Virology, Moscow State University, Moscow 119899, USSR;Institute of Micribiology, Moscow 117811, USSR

关键词: RNA cleavage;    site specific;    Translation;    Nontranslated leader sequence;   

DOI  :  10.1016/0014-5793(89)81010-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Two translationally active fragments were derived from the dicistronic Brome Mosaic Virus (BMV) RNA 3 by site-specific cleavage with RNase H from E.coli: the 5′-proximal (L)fragment encoding the 32 kDa protein and the 3′-proximal (Sh) fragment carrying the coat protein gene. The translational efficiency of the L- and Sh-fragments was compared with those of the native BMV RNA 3 and RNA 4, encoding the 32 kDa and coat proteins, respectively. The Sh-fragment template activity was similar to that of RNA 4, although it was uncapped and contained 20–22 additional 5′-terminal nucleotides in comparison with BMV RNA 4.

【 授权许可】

Unknown