Baxevanis A D, Landsman D
Genome Technology Branch, National Human Genome Research Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
In Silico Biol. 1998;1(1):5-11.
Biochemical studies to date have not been able to identify the linker histone H1 protein in the budding yeast Saccharomyces cerevisiae. Database homology searching against the complete yeast genome has identified a gene, HHO1, (or YPL127C, formerly LPI17) which encodes a protein that has two regions that show similarity to the pea histone H1 globular domain. To determine whether Hho1p can assume the shape of an H1 protein, homology model building experiments were performed using the structure of chicken histone H5 globular domain as the basis for comparison. A statistically significant match between each of the two globular domains of Hho1p and the chicken histone H5 structure was obtained, and probability values indicate that there is a less than 1 in 100 chance that such a match would be the result of a random event. These findings support the proposal that Hho1p acts as an "H1 dimer" and could be responsible for the decreased linker DNA length observed between nucleosomal core particles.
迄今为止,生化研究尚未在芽殖酵母酿酒酵母中鉴定出连接组蛋白H1蛋白。对完整酵母基因组进行数据库同源性搜索,已鉴定出一个基因HHO1(或YPL127C,原名LPI17),该基因编码一种蛋白质,其有两个区域与豌豆组蛋白H1球状结构域相似。为了确定Hho1p是否能呈现H1蛋白的形状,以鸡组蛋白H5球状结构域的结构为比较基础进行了同源性模型构建实验。Hho1p的两个球状结构域与鸡组蛋白H5结构之间均获得了具有统计学意义的匹配,概率值表明这种匹配是随机事件结果的可能性小于1/100。这些发现支持了Hho1p作为“ H1二聚体”发挥作用的提议,并且可能是观察到的核小体核心颗粒之间连接DNA长度减少的原因。