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人巨细胞病毒尿嘧啶 DNA 糖基化酶 UL114 与病毒 DNA 聚合酶催化亚基 UL54 的相互作用。

Interaction of the human cytomegalovirus uracil DNA glycosylase UL114 with the viral DNA polymerase catalytic subunit UL54.

机构信息

Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.

出版信息

J Gen Virol. 2010 Aug;91(Pt 8):2029-2033. doi: 10.1099/vir.0.022160-0. Epub 2010 Apr 21.

Abstract

Interaction between human cytomegalovirus uracil DNA glycosylase (UL114) and the viral DNA polymerase accessory subunit (UL44) has been reported; however, no such association was found in proteomic studies of UL44-interacting proteins. Utilizing virus expressing FLAG-tagged UL114, nuclease-resistant association of UL44 and the DNA polymerase catalytic subunit UL54 with UL114 was observed by co-immunoprecipitation. Contrary to a previous report, we observed that UL114 was much less abundant than UL44. Interaction of UL114 with UL54, independent of the UL54 carboxyl terminus, but not with UL44 was detected in vitro. Our data are consistent with a direct UL114-UL54 interaction, and suggest that UL114 and UL54 act in concert during base excision repair of the viral genome.

摘要

已报道人巨细胞病毒尿嘧啶 DNA 糖基化酶(UL114)与病毒 DNA 聚合酶辅助亚基(UL44)之间存在相互作用;然而,在 UL44 相互作用蛋白的蛋白质组学研究中未发现这种关联。利用表达 FLAG 标签 UL114 的病毒,通过共免疫沉淀观察到 UL44 和 DNA 聚合酶催化亚基 UL54 与 UL114 的核酸酶抗性关联。与之前的报告相反,我们观察到 UL114 的丰度远低于 UL44。在体外检测到 UL114 与 UL54 的相互作用,不依赖于 UL54 的羧基末端,但不与 UL44 相互作用。我们的数据与 UL114-UL54 的直接相互作用一致,并表明 UL114 和 UL54 在病毒基因组的碱基切除修复过程中协同作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/59a9/3052538/6afba5d34f69/2029fig1.jpg

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