Polonskiĭ I S, Kozlov I A, Debabov V G, Zograf I N, Torskiĭ S N
Mol Biol (Mosk). 1976 Jan-Feb;10(1):64-9.
It has been shown that the protein product of T4 bacteriophage gene 32 (protein 32) completely prevents RNA and poly(A) synthesis on the denatured DNA as a template at the protein/DNA ratio about 13:1. Under the same conditions protein 32 has no effect on these syntheses on the native DNA and inhibit poly(A) synthesis with oligo(dT)9 and oligo(dT)12 as a template, preventing binding of enzyme with oligonucleotide. It is possible that the unwinded regions of double-stranded DNA within transcription complexes are too small to allow cooperative binding of protein 32 or are unavailable for this protein. We suppose that the protein 32 and other "unwinding" protein plays not only "protective" and "structural" roles but also participates in the regulation of template activity of single-stranded DNA regions in the replicative forks.
已表明,T4噬菌体基因32的蛋白质产物(蛋白质32)在蛋白质/DNA比例约为13:1时,能完全阻止以变性DNA为模板的RNA和多聚腺苷酸(poly(A))合成。在相同条件下,蛋白质32对以天然DNA为模板的这些合成没有影响,并且抑制以寡聚(dT)9和寡聚(dT)12为模板的多聚腺苷酸合成,阻止酶与寡核苷酸结合。转录复合物内双链DNA的解旋区域可能太小,无法允许蛋白质32协同结合,或者该蛋白质无法利用。我们推测,蛋白质32和其他“解旋”蛋白质不仅发挥“保护”和“结构”作用,还参与复制叉中单链DNA区域模板活性的调节。