测定全长人 PIF1 ATP 酶的生化特性。
Determination of the biochemical properties of full-length human PIF1 ATPase.
机构信息
Department of Radiation Toxicology and Oncology; Beijing Institute of Radiation Medicine; Beijing, PR China; School of Medicine; Shihezi University; Shihezi, PR China.
出版信息
Prion. 2013 Jul-Aug;7(4):341-7. doi: 10.4161/pri.26022. Epub 2013 Aug 7.
The PIF1 helicase family performs many cellular functions. To better understand the functions of the human PIF1 helicase, we characterized the biochemical properties of its ATPase. PIF1 is very sensitive to temperature, whereas it is not affected by pH, and the ATPase activity of human PIF1 is dependent on the divalent cations Mg (2+) and Mn (2+) but not Ca (2+) and Zn (2+). Inhibition was observed when single-stranded DNA was coated with RPA or SSB. Moreover, the ATPase activity of PIF1 proportionally decreased with decreasing oligonucleotide length due to a decreased binding ability. A minimum of 10 oligonucleotide bases are required for PIF1 binding and the hydrolysis of ATP. The analysis of the biochemical properties of PIF1 together with numerous genetic observations should aid in the understanding of its cellular functions.
PIF1 解旋酶家族执行许多细胞功能。为了更好地了解人类 PIF1 解旋酶的功能，我们对其 ATP 酶的生化特性进行了表征。PIF1 对温度非常敏感，而不受 pH 值影响，并且人 PIF1 的 ATP 酶活性依赖于二价阳离子 Mg（2+）和 Mn（2+），而不是 Ca（2+）和 Zn（2+）。当单链 DNA 被 RPA 或 SSB 覆盖时，观察到抑制。此外，由于结合能力降低，PIF1 的 ATP 酶活性随寡核苷酸长度的减少而成比例降低。PIF1 结合和 ATP 水解至少需要 10 个寡核苷酸碱基。对 PIF1 的生化特性的分析以及许多遗传观察结果应该有助于理解其细胞功能。
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