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首页> 外文期刊>Nucleic Acids Research >CHARACTERIZATION OF THE SINGLE-STRAND-SPECIFIC BPV-1 ORIGIN BINDING PROTEIN, SPSF I, AS THE HELA PUR-ALPHA FACTOR
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CHARACTERIZATION OF THE SINGLE-STRAND-SPECIFIC BPV-1 ORIGIN BINDING PROTEIN, SPSF I, AS THE HELA PUR-ALPHA FACTOR

机译：单链特异的BPV-1原始结合蛋白SPSF I的表征，其为HELApur-α因子

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摘要

SPSF I and II are two cellular proteins which bind specifically to single-stranded DNA. SPSF I and II binding sites are found in the minimal origin of replication of BPV-1 DNA and near the P2 promoter of the cellular c-myc gene. DNA-binding properties of the two proteins to single-stranded oligonucleotides of different lengths and sequences were quantified by determination of DNA-binding constants. The binding constant of SPSF proteins to the lower strand of the BPV-1 origin was determined to be 1.5 x 10(-10) M-1. Peptide sequences derived from purified SPSF I and II revealed the identity of at least one of the SPSF proteins with the so-called HeLa Pur alpha factor. The HeLa Pur alpha factor was identified previously by virtue of its capacity to bind to purine-rich strands of the PUR element found in initiation zones of DNA replication [Bergemann,A.D., Ma,Z.-W. and Johnson,E.M. (1992) Mol. Cell. Biol. 12, 5673-5682]. Expression of the Pur cDNA confirmed the identity of the Pur alpha protein with the 42 kDa SPSF I protein. Analysis of several Pur alpha cDNA clones revealed the existence of an extended 3'-untranslated region in all Pur mRNAs.
机译：SPSF I和SPSF是两种细胞蛋白，可特异性结合单链DNA。 SPSF I和II结合位点存在于BPV-1 DNA复制的最小起点中，并且位于细胞c-myc基因的P2启动子附近。通过测定DNA结合常数来定量两种蛋白质与不同长度和序列的单链寡核苷酸的DNA结合特性。 SPSF蛋白与BPV-1来源的下链的结合常数确定为1.5 x 10（-10）M-1。源自纯化的SPSF I和II的肽序列揭示了至少一种SPSF蛋白与所谓的HeLa Purα因子的同一性。 HeLa Purα因子先前凭借其结合在DNA复制起始区中发现的PUR元素的富嘌呤链的能力而得到鉴定[Bergemann，A.D。，Ma，Z.-W。和约翰逊（E.M.） （1992）Mol。细胞。生物学12，5673-5682]。 Pur cDNA的表达证实了Pur alpha蛋白与42 kDa SPSF I蛋白的身份。几个Pur alpha cDNA克隆的分析显示，在所有Pur mRNA中均存在延伸的3'-非翻译区。

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