Response to Comment on "A histone acetylation switch regulates H2A.Z deposition by the SWR-C remodeling enzyme".

Response to Comment on "A histone acetylation switch regulates H2A.Z deposition by the SWR-C remodeling enzyme".
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DOI:
10.1126/science.aad6398
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发表时间:
2016-07-22
期刊:
Science (New York, N.Y.)
影响因子:
--
通讯作者:
Peterson CL
Peterson CL
中科院分区:
其他
文献类型:
--
作者:
Watanabe S;Peterson CL

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Wang等人报道了未能重现我们的生物化学观察结果,即当底物含有H3-K56 Q时,INO 80 C和SWR 1C/SWR 1/SWR-C染色质重塑酶催化核小体H2A.Z被H2 A取代。他们指出我们的二聚体交换试验存在技术问题。作为回应,我们使用Wang及其同事开发和使用的迁移率变化测定法概括了我们的发现。我们使用直接电泳迁移率变动分析来证实当核小体底物含有H3-K56 Q时,INO 80 C催化H2 A. Z与H2 A的置换。
Wang et al. report a failure to reproduce our biochemical observation that the INO80C and SWR1C/SWR1/SWR-C chromatin remodeling enzymes catalyze replacement of nucleosomal H2A.Z with H2A when the substrate contains H3-K56Q. They point to technical problems with our dimer exchange assay. In response, we have recapitulated our findings using a mobility shift assay that was developed and employed by Wang and colleagues. We use a direct electrophoretic mobility shift assay to confirm that INO80C catalyzes the replacement of nucleosomal H2A.Z with H2A when the nucleosomal substrate contains H3-K56Q.
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