Characterization of a telomere-binding protein from Physarum polycephalum.
Characterization of a telomere-binding protein from Physarum polycephalum.
复制标题
多头绒泡菌端粒结合蛋白的表征。
DOI：
10.1128/mcb.11.4.2282-2290.1991
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发表时间：
1991
影响因子：
5.3
通讯作者：
Vogt,VM
中科院分区：
文献类型：
--
作者：
Coren,JS;Epstein,EM;Vogt,VM
我们从多头绒泡菌（Physarumpolycephalum）中部分纯化了一种核蛋白（PPT），它与这种非细胞黏菌的染色体外核糖体DNA端粒结合。结合是特异性的（T2AG3）ntelomere重复，证明了硝酸纤维素过滤器结合试验，凝胶迁移率变动分析与DNA片段和双链寡核苷酸，和DNA酶I足迹。PPT具有显著的热稳定性，在90°C孵育后显示出不减弱的结合活性。它在1.2S处沉淀，对应于约10，000的分子量（对于球状蛋白），并且其结合活性在与RNase孵育时不减弱，这表明它不是核糖核蛋白。我们假设PPT在端粒中起着结构性作用，可能通过端粒特异性末端转移酶阻止核溶解降解或促进端粒延伸。
We have partially purified a nuclear protein (PPT) fromPhysarum polycephalumthat binds to the extrachromosomal ribosomal DNA telomeres of this acellular slime mold. Binding is specific for the (T2AG3)ntelomere repeats, as evidenced by nitrocellulose filter binding assays, by gel mobility shift assays with both DNA fragments and double-stranded oligonucleotides, and by DNase I footprinting. PPT is remarkably heat stable, showing undiminished binding activity after incubation at 90°C. It sediments at 1.2S, corresponding to a molecular weight of about 10,000 (for a globular protein), and its binding activity is undiminished by incubation with RNase, suggesting that it is not a ribonucleoprotein. We hypothesize that PPT plays a structural role in telomeres, perhaps preventing nucleolytic degradation or promoting telomere extension by a telomere-specific terminal transferase.