Kwan S W, Brawerman G
Proc Natl Acad Sci U S A. 1972 Nov;69(11):3247-50. doi: 10.1073/pnas.69.11.3247.
A structure consisting of poly(A) complexed with other components is released from polysomes by ribonuclease treatment. The poly(A) complex has a sedimentation value of 12-15, while the corresponding sedimentation value for free poly(A) is 4. The complex does not appear to represent an artifact formed by interaction of free poly(A) with either cytoplasmic or polysomal proteins. The polynucleotide released from the complex by treatment with sodium dodecyl sulfate shows the same electrophoretic mobility as that of poly(A) isolated from deproteinized polysomal RNA. The poly(A) in the complex is partially protected from digestion by T(2) ribonuclease. At least part of the poly(A) is available for base pairing with poly(U). The components associated with the poly(A) cause it to bind to Millipore filters at low ionic strength. These components are removed from the complex by Pronase digestion. The findings indicate that the poly(A) segment in messenger RNA serves as a binding site for a particle. This particle appears to consist of proteins.
一种由多聚腺苷酸(poly(A))与其他成分复合而成的结构,经核糖核酸酶处理后从多核糖体中释放出来。该多聚腺苷酸复合物的沉降值为12 - 15,而游离多聚腺苷酸的相应沉降值为4。该复合物似乎并非游离多聚腺苷酸与细胞质或多核糖体蛋白相互作用形成的假象。用十二烷基硫酸钠处理从复合物中释放出的多核苷酸,其电泳迁移率与从脱蛋白多核糖体RNA中分离出的多聚腺苷酸相同。复合物中的多聚腺苷酸受到T(2)核糖核酸酶消化的部分保护。至少部分多聚腺苷酸可用于与聚尿苷酸(poly(U))碱基配对。与多聚腺苷酸相关的成分使其在低离子强度下能与微孔滤膜结合。这些成分经链霉蛋白酶消化后从复合物中去除。这些发现表明,信使核糖核酸中的多聚腺苷酸片段充当了一个颗粒的结合位点。这个颗粒似乎由蛋白质组成。