Zhang Aixia, Wassarman Karen M, Ortega Joaquin, Steven Alasdair C, Storz Gisela
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892, USA.
Mol Cell. 2002 Jan;9(1):11-22. doi: 10.1016/s1097-2765(01)00437-3.
The Escherichia coli host factor I, Hfq, binds to many small regulatory RNAs and is required for OxyS RNA repression of fhlA and rpoS mRNA translation. Here we report that Hfq is a bacterial homolog of the Sm and Sm-like proteins integral to RNA processing and mRNA degradation complexes in eukaryotic cells. Hfq exhibits the hallmark features of Sm and Sm-like proteins: the Sm1 sequence motif, a multisubunit ring structure (in this case a homomeric hexamer), and preferential binding to polyU. We also show that Hfq increases the OxyS RNA interaction with its target messages and propose that the enhancement of RNA-RNA pairing may be a general function of Hfq, Sm, and Sm-like proteins.
大肠杆菌宿主因子I（Hfq）可与许多小调控RNA结合，是OxyS RNA抑制fhlA和rpoS mRNA翻译所必需的。我们在此报告，Hfq是真核细胞中RNA加工和mRNA降解复合体不可或缺的Sm和Sm样蛋白的细菌同源物。Hfq具有Sm和Sm样蛋白的标志性特征：Sm1序列基序、多亚基环状结构（在此情况下为同聚六聚体）以及对聚U的优先结合。我们还表明，Hfq增强了OxyS RNA与其靶标信息的相互作用，并提出RNA-RNA配对的增强可能是Hfq、Sm和Sm样蛋白的普遍功能。
