Histones and chromatin structure in hyperthermophilic Archaea.
Histones and chromatin structure in hyperthermophilic Archaea.
复制标题
超嗜热古细菌中的组蛋白和染色质结构。
DOI：
10.1111/j.1574-6976.1996.tb00237.x
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发表时间：
1996
影响因子：
11.3
通讯作者：
Reeve,JN
中科院分区：
文献类型：
--
作者：
Grayling,RA;Sandman,K;Reeve,JN
HMf是来自超嗜热甲烷热菌的组蛋白。它是古细菌组蛋白家族的原型和研究最多的成员，具有与真核小体核心组蛋白相同的一级序列和三维结构，并将DNA分子结合和压缩成核小体样结构（NLS）。HMf制剂是两种类似的小（约7.5 kDa）多肽的混合物，命名为HMfA和HMfB，在体内形成同源二聚体和异源二聚体。HMfA的合成占主导地位，在指数增长，但HMfB的相对量增加M。fervidus细胞进入稳定生长期。对重组体（r）（HMfA）2和（rHMfB）2均质制备物的分析表明，这些蛋白在体外具有不同的DNA结合和压缩特性，这与（HMfA）2、（HMfB）2和HMfA · HMfB二聚体以及它们形成的NLS在调节基因表达和基因组压缩及稳定性方面的不同作用一致。
HMf is a histone from the hyperthermophileMethanothermus fervidus. It is the archetype and most studied member of a family of archaeal histones that have primary sequences and three-dimensional structures in common with the eukaryal nucleosome core histones and that bind and compact DNA molecules into nucleosome-like structures (NLS). HMf preparations are mixtures of two similar, small (∼7.5 kDa) polypeptides designated HMfA and HMfB that in vivo form both homodimers and heterodimers. HMfA synthesis predominates during exponential growth but the relative amount of HMfB increases asM. ferviduscells enter the stationary growth phase. Analyses of homogeneous preparations of recombinant (r) (HMfA)2and (rHMfB)2have demonstrated that these proteins have different DNA-binding and compaction properties in vitro, consistent with different roles in vivo for the (HMfA)2, (HMfB)2and HMfA · HMfB dimers, and for the NLS that they form, in regulating gene expression and in genome compaction and stability.