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首页> 外文期刊>Molecular and Cellular Biology >Species-specific functional interactions of DNA polymerase alpha-primase with simian virus 40 (SV40) T antigen require SV40 origin DNA.
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Species-specific functional interactions of DNA polymerase alpha-primase with simian virus 40 (SV40) T antigen require SV40 origin DNA.

机译:DNA聚合酶α-primase与猿猴病毒40(SV40)T抗原的物种特异性功能相互作用需要SV40起源的DNA。

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Physical and functional interactions of simian virus 40 (SV40) and polyomavirus large-T antigens with DNA polymerase alpha-primase were analyzed to elucidate the molecular basis for the species specificity of polymerase alpha-primase in viral DNA replication. SV40 T antigen associated more efficiently with polymerase alpha-primase in crude human extracts than in mouse extracts, while polyomavirus T antigen interacted preferentially with polymerase alpha-primase in mouse extracts. The apparent species specificity of complex formation was not observed when purified polymerase alpha-primases were substituted for the crude extracts. Several functional interactions between T antigen and purified polymerase alpha-primase, including stimulation of primer synthesis and primer elongation on M13 DNA in the presence or absence of the single-stranded DNA binding protein RP-A, also proved to be independent of the species from which polymerase alpha-primase had been purified. However, the human DNA polymerase alpha-primase was specifically required for primosome assembly and primer synthesis on SV40 origin DNA in the presence of T antigen and RP-A.
机译:分析了猿猴病毒40(SV40)和多瘤病毒大T抗原与DNA聚合酶α-引物酶的物理和功能相互作用,以阐明聚合酶α-引物酶在病毒DNA复制中的物种特异性的分子基础。 SV40 T抗原在人的粗提物中与聚合酶α-primase的结合比在小鼠提取物中更有效,而多瘤病毒T抗原优先与小鼠提取物中的聚合酶α-primase相互作用。当用纯化的聚合酶α-primases代替粗提物时,没有观察到复合物形成的明显物种特异性。 T抗原和纯化的聚合酶α-引发酶之间的几种功能相互作用,包括在存在或不存在单链DNA结合蛋白RP-A的情况下,刺激引物合成和M13 DNA上的引物伸长,也被认为与该物种无关已纯化了哪种聚合酶α-引物。但是,在T抗原和RP-A存在的情况下,在SV40来源的DNA上进行primosome组装和引物合成时,特别需要使用人类DNA聚合酶α-primase。

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