The Saccharomyces cerevisiae histone H2A variant Htz1 is acetylated by NuA4
The Saccharomyces cerevisiae histone H2A variant Htz1 is acetylated by NuA4
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DOI：
10.1101/gad.1388106
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发表时间：
2006-03-15
影响因子：
10.5
通讯作者：
Buratowski, S
中科院分区：
文献类型：
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作者：
Keogh, MC;Mennella, TA;Buratowski, S
组蛋白H2A变体H2A。Z （Saccharomyces cerevisiae Htz1）在转录、DNA修复、染色体稳定性和限制性端粒沉默中发挥作用。swr1 -复合物（SWR-C）将Htz1插入染色质中，并与NuA4组蛋白乙酰转移酶共享几个亚基。此外，这两种复合物的突变体共享几种表型，表明它们可能一起起作用。在这里，我们发现在组蛋白被SWR-C组装成染色质后，NuA4使Htz1 lys14 （K14）乙酰化。K14突变体在染色体传递中表现出特异性缺陷，但不影响转录、端粒沉默或DNA修复。功能特异性修饰可能有助于解释染色质的相同成分如何在不同途径中起作用。
The histone H2A variant H2A.Z (Saccharomyces cerevisiae Htz1) plays roles in transcription, DNA repair, chromosome stability, and limiting telomeric silencing. The Swr1-Complex (SWR-C) inserts Htz1 into chromatin and shares several subunits with the NuA4 histone acetyltransferase. Furthermore, mutants of these two complexes share several phenotypes, suggesting they may work together. Here we show that NuA4 acetylates Htz1 Lys 14 (K14) after the histone is assembled into chromatin by the SWR-C. K14 mutants exhibit specific defects in chromosome transmission without affecting transcription, telomeric silencing, or DNA repair. Function-specific modifications may help explain how the same component of chromatin can function in diverse pathways.