Chroboczek J, Pietrzak M, Zagórski W
J Virol. 1973 Aug;12(2):230-40. doi: 10.1128/JVI.12.2.230-240.1973.
The specificity of formation of phage f2 RNA-protein complexes was studied. Complex I contains up to 8 mol of coat protein per 1 mol of RNA. Its formation proceeds equally well in medium (i) without magnesium ions, (ii) containing magnesium ions, (iii) containing 4 mM EDTA, and (iv) at temperatures from 0 to 45 C. Complex II contains up to 200 mol of coat protein per 1 mol of RNA. Its formation is inhibited by the presence of magnesium ions in medium. Formaldehyde- or methoxyamine-treated f2 RNA in which only exposed bases were modified showed a normal pattern of complex II formation, whereas formation of complex I was inhibited or abolished. We conclude that complex I formation involves the interaction between coat protein and specific region of exposed bases in RNA. A possible site of attachment of coat protein is discussed.
研究了噬菌体f2 RNA - 蛋白质复合物形成的特异性。复合物I每1摩尔RNA含有多达8摩尔的外壳蛋白。其形成在以下几种培养基中进行得同样良好:(i)不含镁离子的培养基;(ii)含镁离子的培养基;(iii)含4 mM EDTA的培养基;以及(iv)温度在0至45°C的条件下。复合物II每1摩尔RNA含有多达200摩尔的外壳蛋白。培养基中镁离子的存在会抑制其形成。经甲醛或甲氧基胺处理的f2 RNA,其中只有暴露的碱基被修饰,显示出正常的复合物II形成模式,而复合物I的形成则受到抑制或消除。我们得出结论,复合物I的形成涉及外壳蛋白与RNA中暴露碱基的特定区域之间的相互作用。讨论了外壳蛋白可能的附着位点。