Stöger T, Augusteyn R C, Graw J
GSF-National Research Center for Environment and Health, Institute of Mammalian Genetics, Neuherberg, Germany.
Ophthalmic Res. 1997;29(3):161-71. doi: 10.1159/000268011.
Based upon DNA sequence analysis of the promoters from six gamma-crystallin genes (cryga-->crygf) a 36-bp DNA fragment was defined as 'Cryner' (cryg nested repeat). The presence of these repeats made this structure a candidate for DNA-protein interaction. The present experiments demonstrate interactions of lens proteins with the Cryner element from murine cryga, crygb, crygd and cryge. Additionally, DNA covering the sequence of about 30 nt between Cryner and the TATA-box of the murine crygb exhibits sequence-specific interactions with the bovine alpha-crystallin-containing fraction. The results confirm the hypothesis that the Cryner element is able to interact with lens proteins. It is noteworthy that this interaction is specific for the template strand of the DNA. The present model includes the possibility of sequence-dependent conformational changes leading to various DNA-protein complexes.
基于对六个γ-晶状体蛋白基因（cryga至crygf）启动子的DNA序列分析，一个36碱基对的DNA片段被定义为“Cryner”（cryg嵌套重复序列）。这些重复序列的存在使该结构成为DNA-蛋白质相互作用的候选对象。目前的实验证明了晶状体蛋白与来自小鼠cryga、crygb、crygd和cryge的Cryner元件之间的相互作用。此外，覆盖小鼠crygb的Cryner和TATA框之间约30个核苷酸序列的DNA与含牛α-晶状体蛋白的组分表现出序列特异性相互作用。结果证实了Cryner元件能够与晶状体蛋白相互作用的假说。值得注意的是，这种相互作用对DNA的模板链具有特异性。目前的模型包括序列依赖性构象变化导致各种DNA-蛋白质复合物的可能性。
