Laín S, Riechmann J L, García J A
Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma, Madrid, Spain.
Nucleic Acids Res. 1990 Dec 11;18(23):7003-6. doi: 10.1093/nar/18.23.7003.
Most positive strand RNA viruses infecting plants and animals encode proteins containing the so-called nucleotide binding motif (NTBM) (1) in their amino acid sequences (2). As suggested from the high level of sequence similarity of these viral proteins with the recently described superfamilies of helicase-like proteins (3-5), the NTBM-containing cylindrical inclusion (CI) protein from plum pox virus (PPV), which belongs to the potyvirus group of positive strand RNA viruses, is shown to be able to unwind RNA duplexes. This activity was found to be dependent on the hydrolysis of NTP to NDP and Pi, and thus it can be considered as an RNA helicase activity. In the in vitro assay used, the PPV CI protein was only able to unwind double strand RNA substrates with 3' single strand overhangs. This result indicates that the helicase activity of the PPV CI protein functions in the 3' to 5' direction (6). To our knowledge, this is the first report on a helicase activity associated with a protein encoded by an RNA virus.
大多数感染动植物的正链RNA病毒在其氨基酸序列中编码含有所谓核苷酸结合基序(NTBM)的蛋白质。从这些病毒蛋白与最近描述的解旋酶样蛋白超家族的高度序列相似性可以推测,来自李痘病毒(PPV)的含NTBM的柱状内含体(CI)蛋白,属于正链RNA病毒的马铃薯Y病毒属,被证明能够解开RNA双链体。发现这种活性依赖于NTP水解为NDP和Pi,因此可以将其视为一种RNA解旋酶活性。在所用的体外试验中,PPV CI蛋白仅能够解开具有3'单链突出端的双链RNA底物。该结果表明PPV CI蛋白的解旋酶活性在3'至5'方向起作用。据我们所知,这是关于与RNA病毒编码的蛋白质相关的解旋酶活性的首次报道。