Divalent ions attenuate DNA synthesis by human DNA polymerase α by changing the structure of the template/primer or by perturbing the polymerase reaction
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- 作者：Yinbo Zhanga ; b ; Andrey G. Baranovskiya ; Emin T. Tahirova ; 1 ; Tahir H. Tahirova ; ttahirov@unmc.edu" class="auth_mail" title="E-mail the corresponding author ; Youri I. Pavlova ; b ; c ; ypavlov@unmc.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：pol ; DNA polymerase ; polα-prim ; four subunit human polα-primase ; polδ DNA ; polymerase δ ; polε ; DNA polymerase ε ; Me2+ ; divalent metal cation ; polα-core ; catalytic domain of human polα
- 刊名：DNA Repair
- 出版年：2016
- 出版时间：July 2016
- 年：2016
- 卷：43
- 期：Complete
- 页码：24-33
- 全文大小：2254 K
文摘
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Mg2+ at suboptimal concentration inhibited DNA polα and several other pols on templates with repetitive sequence by stabilizing unconventional DNA structure(s).
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Zn2+ supported DNA synthesis reactions by polα with low efficiency, but inhibited synthesis when Mg2+ was present, suggesting the possibility that the step of removal of divalent metal ions after the formation of the phosphodiester bond is critical for polymerase reaction.
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The balance of the divalent metal ions is critical for the efficient DNA polymerase function.