Biophysical and biochemical characterization of recombinant human Pop2 deadenylase
Biophysical and biochemical characterization of recombinant human Pop2 deadenylase
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重组人 Pop2 去腺苷酸酶的生物物理和生化表征
DOI：
10.1016/j.pep.2008.03.008
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发表时间：
2008-07-01
影响因子：
1.6
通讯作者：
Yan, Yong-Bin
中科院分区：
文献类型：
--
作者：
Liu, Wei-Feng;Yan, Yong-Bin
Pop 2是Ccr 4-Not复合物的一种组分，在体外和体内都起脱腺苷酶的作用。本研究发现，重组人Pop 2（hPop 2）主要以α + β三级结构的紧凑单体状态存在。从CD光谱评价的二级结构的百分比为约37% α-螺旋、14% β-折叠和19% β-转角。hPop 2催化的最佳条件为37 ℃、pH 7-8。Mg ~（2+）、Mn ~（2+）和Co ~（2+）对hPop 2去腺苷化酶活性的影响相似，最适浓度为0.3-0.5 mM，当与二价金属离子配位时，hPop 2去腺苷化酶活性至少部分具有专一性。该酶不受核体类似物的抑制，产物5 '-AMP是最有效的抑制剂。不同的金属离子依赖性和抑制作用的核体类似物的不同建议，不同的deadenylases可能有不同的调节机制。(c)2008年爱思唯尔公司All rights reserved.
Pop2, a component of the Ccr4-Not complex, functions as a deadenylase both in vitro and in vivo. In this research, we found that the recombinant human Pop2 (hPop2) mainly existed in a compact monomeric state with a alpha + beta tertiary structure type. The percentages of the secondary structures evaluated from the CD spectrum were about 37% alpha-helix, 14% beta-sheet, and 19% beta-turns. The optimal condition for hPop2 catalysis was pH 7-8 at 37 degrees C. Mg2+, Mn2+ and Co2+ had similar effects on the deadenylation activity of hPop2, and the optimal concentration was 0.3-0.5 mM. The deadenylase activity of hPop2 was, at least partially, specific when coordinated with divalent metal ions. The enzyme was not inhibited much by the nucleoticle analogs, and the product 5'-AMP was the most efficient inhibitor. The dissimilarity in the metal ion dependence and inhibitory effects of the nucleoticle analogs suggested that various deadenylases might have differential regulation mechanisms. (c) 2008 Elsevier Inc. All rights reserved.