Identification of maize histone deacetylase HD2 as an acidic nucleolar phosphoprotein
Identification of maize histone deacetylase HD2 as an acidic nucleolar phosphoprotein
复制标题
DOI：
10.1126/science.277.5322.88
复制
发表时间：
1997-07-04
期刊：
影响因子：
56.9
通讯作者：
Loidl, P
中科院分区：
文献类型：
--
作者：
Lusser, A;Brosch, G;Loidl, P
组蛋白乙酰化的稳态是由多种组蛋白乙酰转移酶和脱乙酰酶建立和维持的，这种稳态影响染色质的结构和功能。本文报道了一种编码染色质结合脱乙酰酶HD2的玉米互补DNA的鉴定。该蛋白与酵母RPD 3转录调节因子不同源。它在整个胚胎萌发过程中表达，与细胞的增殖活性相关。针对重组HD2-p39的抗体免疫沉淀天然酶复合物，其由磷酸化的p39亚基组成。免疫荧光显微镜和序列同源性表明核仁定位。HD2是一种酸性核仁磷蛋白，可能调节核糖体染色质的结构和功能。
The steady state of histone acetylation is established and maintained by multiple histone acetyltransferases and deacetylases, and this steady state affects chromatin structure and function. The identification of a maize complementary DNA encoding the chromatin-bound deacetylase HD2 is reported. This protein was not homologous to the yeast RPD3 transcriptional regulator. It was expressed throughout embryo germination in correlation with the proliferative activity of cells. Antibodies against recombinant HD2-p39 immunoprecipitated the native enzyme complex, which was composed of phosphorylated p39 subunits. Immunofluorescence microscopy and sequence homologies suggested nucleolar localization. HD2 is an acidic nucleolar phosphoprotein that might regulate ribosomal chromatin structure and function.