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首页> 外文期刊>Biochemistry >Human DNA primase: anion inhibition, manganese stimulation, and their effects on in vitro start-site selection.
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Human DNA primase: anion inhibition, manganese stimulation, and their effects on in vitro start-site selection.

机译：人类DNA引发酶：阴离子抑制，锰刺激及其对体外起始位点选择的影响。

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摘要

We examined the effects of Mn(2+) on eukaryotic DNA primase both in the presence and absence of 5 mM Mg(2+). In the absence of Mg(2+), Mn(2+)-supported primase activity to a level 4-fold greater than that obtained with Mg(2+) alone, and adding low levels of Mn(2+) (100 microM) to assays containing 5 mM Mg(2+) greatly stimulated primase. Increased activity was primarily due to more efficient utilization of NTPs, as reflected in a lower K(M) for NTPs. Under conditions of saturating NTPs, Mn(2+) had minimal effects on both the rate of initiation (i.e., dinucleotide synthesis) and processivity. The effects of Mn(2+) involve multiple metal binding sites on primase and may involve both the catalytic p49 subunit as well as the p58 subunit. Physiological levels of salt can inhibit primase activity due to the presence of an anion binding site and low levels of Mn(2+) significantly decreased this salt sensitivity. The implications of these results with respect to the biological role of primase are discussed.
机译：我们在有和没有5 mM Mg（2+）的情况下检查了Mn（2+）对真核DNA primase的影响。在没有Mg（2+）的情况下，Mn（2+）支持的启动酶活性比单独使用Mg（2+）获得的酶高4倍，并添加了低水平的Mn（2+）（100 microM ）到含有5 mM Mg（2+）的试验中大大刺激的引发酶。活动的增加主要归因于NTP的更有效利用，这反映为NTP的K（M）较低。在NTP饱和的条件下，Mn（2+）对引发速率（即二核苷酸合成）和合成能力的影响最小。 Mn（2+）的影响涉及在primase上的多个金属结合位点，并可能涉及催化的p49亚基和p58亚基。盐的生理水平可以抑制由于阴离子结合位点的存在而引起的蛋白酶活性，而低水平的Mn（2+）则明显降低了该盐的敏感性。讨论了这些结果对引发酶的生物学作用的影响。

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