Yeast Srp1p has homology to armadillo/plakoglobin/beta-catenin and participates in apparently multiple nuclear functions including the maintenance of the nucleolar structure.
Yeast Srp1p has homology to armadillo/plakoglobin/beta-catenin and participates in apparently multiple nuclear functions including the maintenance of the nucleolar structure.
复制标题
酵母 Srp1p 与犰狳/斑球蛋白/β-连环蛋白具有同源性，并参与明显的多种核功能，包括维持核仁结构。
DOI：
10.1073/pnas.91.15.6880
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发表时间：
1994
影响因子：
11.1
通讯作者：
Nomura,M
中科院分区：
文献类型：
--
作者：
Yano,R;Oakes,ML;Tabb,MM;Nomura,M
SRP1 是酿酒酵母 RNA 聚合酶 I 某些温度敏感突变的抑制因子，编码与核孔相关的蛋白质。通过使用条件 SRP1 表达系统并分离温度敏感的 srp1 突变体，我们证明 Srp1p 对于维持新月形核仁结构、RNA 转录以及微管的正常功能（从核分裂/分离和微管免疫荧光显微镜分析推断）至关重要。与蛋白质的这些明显的多种功能作用相关，不同的突变等位基因表现出显着不同的表型。我们还发现，Srp1p 中存在的 8 个不完美的 42 个氨基酸串联重复序列与高等真核生物粘附连接复合物中存在的犰狳/斑球蛋白/β-连环蛋白中的 42 个氨基酸重复序列相似。我们结合观察到的 srp1 突变的多效性效应来讨论这种相似性。
SRP1, a suppressor of certain temperature-sensitive mutations in RNA polymerase I in Saccharomyces cerevisiae, encodes a protein that is associated with nuclear pores. By using a system of conditional SRP1 expression and by isolating temperature-sensitive srp1 mutants, we have demonstrated that Srp1p is essential for maintenance of the crescent-shaped nucleolar structure, RNA transcription, and the proper functions of microtubules as inferred from analysis of nuclear division/segregation and immunofluorescence microscopy of microtubules. Different mutant alleles showed significantly different phenotypes in relation to these apparently multiple functional roles of the protein. We have also found that eight imperfect 42-amino-acid tandem repeats present in Srp1p are similar to the 42-amino-acid repeats in armadillo/plakoglobin/beta-catenin proteins present in adhesive junction complexes of higher eukaryotes. We discuss this similarity in connection with the observed pleiotropic effects of srp1 mutations.