Rudt F, Pieler T
Institut für Biochemie und Molekulare Zellbiologie, Göttingen, Germany.
EMBO J. 1996 Mar 15;15(6):1383-91.
Nuclear export of newly transcribed 5S ribosomal RNA in Xenopus oocytes occurs in the context of either a complex with the ribosomal protein L5 (5S RNP) or with the transcription factor IIIA (7S RNP). Here we examine nuclear import of 5S RNA, L5 and TFIIIA. The 5S RNP shuttles between nucleus and cytoplasm and only 5S RNA variants which can bind to L5 gain access to the nucleus. The 7S RNP is retained in the cytoplasm. Only TFIIIA which is not bound to 5S RNA is imported into the nucleus. As a novel mechanism for cytoplasmic retention, we propose that RNA binding masks a nuclear localization sequence in TFIIIA. In contrast to the nuclear import of L5, import of TFIIIA is sensitive towards the nuclear localization sequence (NLS) competitor p(lys)-BSA, suggesting that these two proteins make use of different import pathways.
非洲爪蟾卵母细胞中新转录的5S核糖体RNA的核输出发生在与核糖体蛋白L5(5S核糖核蛋白)或转录因子IIIA(7S核糖核蛋白)形成复合物的情况下。在此,我们研究5S RNA、L5和TFIIIA的核输入。5S核糖核蛋白在细胞核和细胞质之间穿梭,只有能与L5结合的5S RNA变体才能进入细胞核。7S核糖核蛋白保留在细胞质中。只有未与5S RNA结合的TFIIIA被导入细胞核。作为一种新的细胞质保留机制,我们提出RNA结合会掩盖TFIIIA中的一个核定位序列。与L5的核输入不同,TFIIIA的输入对核定位序列(NLS)竞争者聚(赖氨酸)-牛血清白蛋白敏感,这表明这两种蛋白质利用不同的输入途径。