FEBS Letters | |
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 | |
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
【 预 览 】
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