Thomas J O, Szer W
Nucleic Acids Res. 1982 Dec 11;10(23):7777-89. doi: 10.1093/nar/10.23.7777.
Glycine-rich core hnRNP proteins purified from wheat bind tightly to single-stranded but not to double-stranded nucleic acids with a preference for natural RNA over single-stranded DNA. Binding results in i) a progressive disruption of the residual secondary structure of the polynucleotide and the formation of an extended nucleoprotein filament until a protein to polynucleotide weight ratio of about 5:1 is attained. As more protein is added, this is followed by ii) the formation of globular structures along the polynucleotide chain with a concomitant reduction in the contour length of the nucleoprotein complex. These two features of the interaction--unwinding and condensation into beads--are analogous to the previously described behavior of the major glycine-rich core hnRNP protein from Artemia salina (Thomas et al. (1981) Proc. Natl. Acad. Sci. USA 78, 2888) and may represent the basic functional properties of this relatively well conserved group of nuclear proteins.
从小麦中纯化出的富含甘氨酸核心的核不均一核糖核蛋白（hnRNP）能紧密结合单链核酸，但不结合双链核酸，且相较于单链DNA，更倾向于结合天然RNA。这种结合会导致：i）多核苷酸残留二级结构逐渐被破坏，并形成延伸的核蛋白细丝，直至蛋白质与多核苷酸的重量比达到约5:1。随着更多蛋白质的加入，接着会出现ii）沿着多核苷酸链形成球状结构，同时核蛋白复合物的轮廓长度缩短。这种相互作用的两个特征——解旋并聚集成珠状——类似于先前描述的卤虫主要富含甘氨酸核心的hnRNP蛋白的行为（Thomas等人，（1981年）《美国国家科学院院刊》78, 2888），可能代表了这一相对保守的核蛋白组的基本功能特性。
