Identification of cis-acting sites for condensin loading onto budding yeast chromosomes
Identification of cis-acting sites for condensin loading onto budding yeast chromosomes
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DOI：
10.1101/gad.1675708
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发表时间：
2008-08-15
影响因子：
10.5
通讯作者：
Uhlmann, Frank
中科院分区：
文献类型：
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作者：
D'Ambrosio, Claudio;Schmidt, Christine Katrin;Uhlmann, Frank
真核染色体取决于进化保守的冷凝蛋白复合物的反应，在有丝分裂中达到稳定的杆状外观。关于如何和位于凝结蛋白与染色体相关的地方知之甚少。在这里，我们使用高分辨率寡核苷酸瓷砖阵列分析了与出现的酵母染色体结合的冷凝蛋白。冷凝蛋白结合位点与相关粘着蛋白复合物的负载因子SCC2/4的结合位点一致。这些位点映射到tRNA和其他基因，由RNA聚合酶III转录因子TFIIIC，核糖体蛋白和SNR基因映射。由TFIIIC识别的异位B-box元件构成最小的冷凝蛋白结合位点，而TFIIIC和SCC2/4复合物促进了功能性公寓蛋白与染色体相关性。沿裂变酵母染色体保守的冷凝蛋白结合模式。这表明TFIIIC结合位点（包括tRNA基因）构成了迄今未知的染色体特征，对相间和有丝分裂过程中染色体结构具有重要意义。
Eukaryotic chromosomes reach their stable rod-shaped appearance in mitosis in a reaction dependent on the evolutionarily conserved condensin complex. Little is known about how and where condensin associates with chromosomes. Here, we analyze condensin binding to budding yeast chromosomes using high-resolution oligonucleotide tiling arrays. Condensin-binding sites coincide with those of the loading factor Scc2/4 of the related cohesin complex. The sites map to tRNA and other genes bound by the RNA polymerase III transcription factor TFIIIC, and ribosomal protein and SNR genes. An ectopic B-box element, recognized by TFIIIC, constitutes a minimal condensin-binding site, and TFIIIC and the Scc2/4 complex promote functional condensin association with chromosomes. A similar pattern of condensin binding is conserved along fission yeast chromosomes. This reveals that TFIIIC-binding sites, including tRNA genes, constitute a hitherto unknown chromosomal feature with important implications for chromosome architecture during both interphase and mitosis.