Swamynathan S K, Nambiar A, Guntaka R V
Department of Molecular Microbiology and Immunology, School of Medicine, University of Missouri-Columbia, Columbia, MO 65212, USA.
Biochem J. 2000 Jun 1;348 Pt 2(Pt 2):297-305.
Y-Box proteins comprise a large family of multifunctional proteins with a wide spectrum of activities in both transcription and translational regulation of gene expression. Earlier, we have reported on the involvement of chk-YB-2 in transcriptional regulation of Rous sarcoma virus long terminal repeats and the involvement of chk-YB-1b in transcriptional regulation of alpha1(I) collagen genes. Here, we have investigated the potential role of chk-YB-2 and chk-YB-1b in RNA metabolism. We report that chk-YB-2 and chk-YB-1b are localized predominantly in the cytoplasm and that they both can bind single-stranded RNA in a sequence-specific and reversible manner. Well-conserved cold-shock domain, N-terminal proline-rich domain and the alternating clusters of acidic and basic amino acids located in the C-terminal ends of these two proteins were all found to be necessary for their RNA-binding ability. Further, we demonstrate that these two proteins inhibit translation in vitro and that binding to RNA is required for this inhibition. The significance of these results is discussed.
Y盒蛋白构成了一个多功能蛋白的大家族,在基因表达的转录和翻译调控中具有广泛的活性。此前,我们报道了chk-YB-2参与劳氏肉瘤病毒长末端重复序列的转录调控,以及chk-YB-1b参与α1(I)胶原基因的转录调控。在此,我们研究了chk-YB-2和chk-YB-1b在RNA代谢中的潜在作用。我们报道,chk-YB-2和chk-YB-1b主要定位于细胞质中,并且它们都能以序列特异性和可逆的方式结合单链RNA。发现这两种蛋白质C末端保守的冷休克结构域、N末端富含脯氨酸的结构域以及酸性和碱性氨基酸的交替簇对于它们的RNA结合能力都是必需的。此外,我们证明这两种蛋白质在体外抑制翻译,并且这种抑制需要与RNA结合。讨论了这些结果的意义。