Tacke E, Prüfer D, Schmitz J, Rohde W
Max-Planck-Institut für Züchtungsforschung, Köln, Germany.
J Gen Virol. 1991 Aug;72 ( Pt 8):2035-8. doi: 10.1099/0022-1317-72-8-2035.
The potato leafroll luteovirus protein of Mr 17K (pr17), which is encoded by an open reading frame on the 3' half of the viral genome, was expressed by using bacterial expression vector systems. Fusion proteins were obtained for the full-length viral protein as well as its N-terminal acidic (GST/pr17N) and C-proximal (GST/pr17C) basic domains and used in nucleic acid-binding studies. Filter-bound as well as soluble pr17 bound to single-stranded RNA or DNA. The binding domain was shown to reside in the basic C-proximal part of the polypeptide, whereas the N-terminal acidic domain did not show any affinity for nucleic acid. These biochemical properties of pr17 together with its structural features suggest a regulatory role for this protein during virus replication.
由病毒基因组3' 端的一个开放阅读框编码的分子量为17K的马铃薯卷叶黄化病毒蛋白（pr17），通过细菌表达载体系统进行表达。获得了全长病毒蛋白及其N端酸性结构域（GST/pr17N）和C端碱性结构域（GST/pr17C）的融合蛋白，并用于核酸结合研究。与单链RNA或DNA结合的滤膜结合型以及可溶性pr17均被检测到。结合结构域位于多肽的C端碱性部分，而N端酸性结构域对核酸没有任何亲和力。pr17的这些生化特性及其结构特征表明该蛋白在病毒复制过程中具有调节作用。
