Tacke E, Schmitz J, Prüfer D, Rohde W
Max-Planck-Institut für Züchtungsforschung, Köln, Germany.
Virology. 1993 Nov;197(1):274-82. doi: 10.1006/viro.1993.1588.
The 17 kDa protein (pr17) of potato leafroll luteovirus is translated from a subgenomic PLRV RNA by internal translation initiation and binds to single-stranded nucleic acids (E. Tacke, D. Prüfer, J. Schmitz, and E. Rohde, 1991, J. Gen. Virol. 72, 2035-2038). Chemical crosslinking of in vitro expressed pr17 provided evidence for the preferential formation of pr17 homodimers which were also detected in PLRV-infected potato plants and isolated from potato lines expressing the PLRV pr17 transgene. Mutation analysis identified an amphipathic alpha-helix within the acidic amino-terminus of pr17 which acts as the domain for protein/protein interactions. Pr17 was predominantly associated with subcellular fractions enriched for nuclei, chloroplasts, mitochondria, and membranous structures. In addition it was shown that pr17 was phosphorylated in planta and that this modification did not inhibit binding of the protein to nucleic acids.
马铃薯卷叶黄化病毒的17 kDa蛋白（pr17）通过内部翻译起始从亚基因组PLRV RNA翻译而来，并与单链核酸结合（E. Tacke、D. Prüfer、J. Schmitz和E. Rohde，1991年，《普通病毒学杂志》72卷，2035 - 2038页）。体外表达的pr17的化学交联为pr17同源二聚体的优先形成提供了证据，这种二聚体也在感染PLRV的马铃薯植株中被检测到，并从表达PLRV pr17转基因的马铃薯品系中分离出来。突变分析确定了pr17酸性氨基末端内的一个两亲性α螺旋，它作为蛋白质/蛋白质相互作用的结构域。Pr17主要与富含细胞核、叶绿体、线粒体和膜结构的亚细胞组分相关。此外，研究表明pr17在植物体内被磷酸化，并且这种修饰并不抑制该蛋白与核酸的结合。
