Muniyappa K, Mythili E
Department of Biochemistry, Indian Institute of Science, Bangalore, India.
Biochem Mol Biol Int. 1993 Sep;31(1):1-11.
We have purified phage lambda beta protein produced by a recombinant plasmid carrying bet gene and confirm that it forms a complex with a protein of relative molecular mass 70 kDa. Therefore, beta protein, a component of general genetic recombination, is associated with two functionally diverse complexes; one containing exonuclease and the other 70 kDa protein. Using a number of independent methods, we show that 70 kDa protein is the ribosomal S1 protein of E. coli. Further, the association of 70 kDa protein with beta protein is biologically significant, as the former inhibits joining of the terminal ends of lambda chromosome and renaturation of complementary single stranded DNA promoted by the latter. More importantly, these findings initiate an understanding of an important mode of host- virus interaction in general with specific implication(s) in homologous genetic recombination.
我们已经纯化了由携带bet基因的重组质粒产生的噬菌体λβ蛋白，并证实它与一种相对分子质量为70 kDa的蛋白质形成了复合物。因此，作为一般遗传重组组分的β蛋白与两种功能不同的复合物相关联；一种含有核酸外切酶，另一种含有70 kDa蛋白。我们使用多种独立方法表明，70 kDa蛋白是大肠杆菌的核糖体S1蛋白。此外，70 kDa蛋白与β蛋白的关联具有生物学意义，因为前者抑制λ染色体末端的连接以及后者促进的互补单链DNA的复性。更重要的是，这些发现开启了对宿主 - 病毒相互作用一般重要模式的理解，并在同源遗传重组中具有特定意义。
