叶绿体包膜膜中PEND蛋白DNA结合结构域的DNA结合特异性和二聚化
DNA-binding specificity and dimerization of the DNA-binding domain of the PEND protein in the chloroplast envelope membrane.
作者信息
Sato N, Ohta N
机构信息
Department of Molecular Biology, Faculty of Science, Saitama University, 255 Shimo-Ohkubo, Saitama, Saitama Prefecture 338-8570, Japan.
出版信息
Nucleic Acids Res. 2001 Jun 1;29(11):2244-50. doi: 10.1093/nar/29.11.2244.
The PEND protein is a DNA-binding protein in the inner envelope membrane of a developing chloroplast, which may anchor chloroplast nucleoids. Here we report the DNA-binding characteristics of the N-terminal basic region plus leucine zipper (bZIP)-like domain of the PEND protein that we call cbZIP domain. The basic region of the cbZIP domain diverges significantly from the basic region of known bZIP proteins that contain a bipartite nuclear localization signal. However, the cbZIP domain has the ability to dimerize in vitro. Selection of binding sites from a random sequence pool indicated that the cbZIP domain preferentially binds to a canonical sequence, TAAGAAGT. The binding site was also confirmed by gel mobility shift analysis using a representative binding site within the chloroplast DNA. These results suggest that the cbZIP domain is a unique DNA-binding domain of the chloroplast protein.
PEND蛋白是发育中的叶绿体内膜中的一种DNA结合蛋白，可能锚定叶绿体类核。在此，我们报告了PEND蛋白N端碱性区域加亮氨酸拉链（bZIP）样结构域（我们称之为cbZIP结构域）的DNA结合特性。cbZIP结构域的碱性区域与含有双分核定位信号的已知bZIP蛋白的碱性区域有显著差异。然而，cbZIP结构域在体外具有二聚化能力。从随机序列库中选择结合位点表明，cbZIP结构域优先结合一个典型序列TAAGAAGT。使用叶绿体DNA内的一个代表性结合位点进行的凝胶迁移率变动分析也证实了该结合位点。这些结果表明，cbZIP结构域是叶绿体蛋白独特的DNA结合结构域。
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