The telomere-binding protein Taz1p as a target for modification by a SUMO-1 homologue in fission yeast
The telomere-binding protein Taz1p as a target for modification by a SUMO-1 homologue in fission yeast
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DOI：
10.1007/s10528-005-1503-4
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发表时间：
2005-04-01
影响因子：
2.4
通讯作者：
Chambers, A
中科院分区：
文献类型：
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作者：
Spink, K;Ho, JCY;Chambers, A
在裂殖酵母（裂殖酵母）中，哺乳动物SUMO-1泛素样修饰物的同源物由pmt 3基因编码。使用端粒结合蛋白Taz 1 p作为诱饵的双杂交筛选确定Pmt 3 p为相互作用因子。在体外实验中使用的裂变酵母Pmt 3 p修饰系统的纯化组分表明，Taz 1 p可以直接修饰Pmt 3 p。Taz 1 p的氨基酸序列与SUMO-1的共有修饰位点密切匹配，并且PEST序列与已建立的SUMO- 1靶标中发现的PEST序列相似。虽然以前的实验已经确定了端粒长度的增加作为一个后果的pmt 3基因型，我们不能检测Pmt 3 p修改Taz 1 p的蛋白质提取物从指数增长的单倍体细胞或任何影响的Pmt 3 p上的本地化的GFP-Taz 1 p在离散的焦点在单倍体细胞核。
In fission yeast ( Schizosaccharomyces pombe) the homologue of the mammalian SUMO-1 ubiquitin-like modifier is encoded by the pmt3 gene. A two-hybrid screen using the telomere-binding protein Taz1p as bait identified Pmt3p as an interacting factor. In vitro experiments using purified components of the fission yeast Pmt3p modification system demonstrated that Taz1p could be modified directly by Pmt3p. The amino acid sequence of Taz1p contains a close match to the consensus modification site for SUMO-1, and a PEST sequence similar to those found in established SUMO- 1 targets. Although previous experiments have identified an increase in telomere length as one consequence of the pmt3-genotype, we could not detect Pmt3p modification of Taz1p in protein extracts made from exponentially growing haploid cells or any effect of Pmt3p on the localization of GFP-Taz1p at discrete foci in the haploid cell nucleus.