真核核糖核酸酶H与花椰菜花叶病毒蛋白共享一个保守结构域，该结构域有助于多顺反子RNA的翻译。
Eukaryotic RNAse H shares a conserved domain with caulimovirus proteins that facilitate translation of polycistronic RNA.
作者信息
Mushegian A R, Edskes H K, Koonin E V
机构信息
Department of Plant Pathology, University of Kentucky, Lexington 40546-0091.
出版信息
Nucleic Acids Res. 1994 Oct 11;22(20):4163-6. doi: 10.1093/nar/22.20.4163.
Abstract
RNAse H (RNH1 protein) from the trypanosomatid Crithidia fasciculata has a functionally uncharacterized N-terminal domain dispensable for the RNAse H activity. Using computer methods for database search and multiple alignment, we show that the N-terminal domains of RNH1 and its homologue encoded by a cDNA from chicken lens are related to the conserved domain in caulimovirus ORF VI product that facilitates translation of polycistronic virus RNA in plant cells. We hypothesize that the N-terminal domain of eukaryotic RNAse H performs an as yet uncharacterized regulatory function, possibly in mRNA translation or turnover.
摘要
来自锥虫类生物纤细短膜虫的核糖核酸酶H（RNH1蛋白）具有一个功能未明确的N端结构域，该结构域对于核糖核酸酶H的活性而言并非必需。通过使用计算机方法进行数据库搜索和多序列比对，我们发现RNH1的N端结构域及其由鸡晶状体cDNA编码的同源物与花椰菜花叶病毒ORF VI产物中的保守结构域相关，该保守结构域有助于植物细胞中多顺反子病毒RNA的翻译。我们推测真核核糖核酸酶H的N端结构域可能在mRNA翻译或周转过程中发挥尚未明确的调节功能。
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本文引用的文献
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Functional complementation of an Escherichia coli ribonuclease H mutation by a cloned genomic fragment from the trypanosomatid Crithidia fasciculata.来自锥虫类克氏锥虫的克隆基因组片段对大肠杆菌核糖核酸酶H突变的功能互补作用。
Proc Natl Acad Sci U S A. 1993 Oct 15;90(20):9350-4. doi: 10.1073/pnas.90.20.9350.
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Characterization of ribonuclease H activities present in two cell-free protein synthesizing systems, the wheat germ extract and the rabbit reticulocyte lysate.对两种无细胞蛋白质合成系统（小麦胚芽提取物和兔网织红细胞裂解物）中存在的核糖核酸酶H活性的表征。
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