Makhov A M
D.I. Ivanovsky Institute of Virology, Academy of Medical Sciences, Moscow, USSR.
FEBS Lett. 1989 Jan 30;243(2):115-8. doi: 10.1016/0014-5793(89)80110-3.
By means of comparative analysis of primary and secondary structures, and hydropathy plots of hepadnavirus P proteins new functional domains were revealed additionally to the polymerase domain which had been found earlier in these proteins. The C-terminal part of P proteins was revealed to be significantly similar to ribonuclease H of E. coli. The ribonuclease H functional domain is known to be an integral entity of retrovirus reverse transcriptase as a rule. Availability of this domain indicates once more the putative reverse transcriptase properties of the P products. The proteins of hepadnaviruses were compared to terminal proteins of picornaviruses, adenoviruses and bacteriophages. The data obtained suggested that a conservative N-terminal region of P proteins functions as protein primer for DNA synthesis in hepadnaviruses.
通过对嗜肝DNA病毒P蛋白的一级和二级结构以及亲水性图谱进行比较分析，除了先前在这些蛋白中发现的聚合酶结构域外，还揭示了新的功能域。P蛋白的C末端部分被发现与大肠杆菌的核糖核酸酶H显著相似。众所周知，核糖核酸酶H功能域通常是逆转录病毒逆转录酶的一个组成部分。该结构域的存在再次表明P产物具有推定的逆转录酶特性。将嗜肝DNA病毒的蛋白与小RNA病毒、腺病毒和噬菌体的末端蛋白进行了比较。所得数据表明，P蛋白保守的N末端区域在嗜肝DNA病毒中作为DNA合成的蛋白质引物发挥作用。
