Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2021609 | Protein Expression and Purification | 2008 | 7 Pages |
Abstract
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 α + β tertiary structure type. The percentages of the secondary structures evaluated from the CD spectrum were about 37% α-helix, 14% β-sheet, and 19% β-turns. The optimal condition for hPop2 catalysis was pH 7-8 at 37 °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 nucleotide analogs, and the product 5â²-AMP was the most efficient inhibitor. The dissimilarity in the metal ion dependence and inhibitory effects of the nucleotide analogs suggested that various deadenylases might have differential regulation mechanisms.
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Authors
Wei-Feng Liu, Yong-Bin Yan,