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球形棕囊藻病毒 DNA 聚合酶 X：一把“瑞士军刀”，碱基切除修复的多功能 DNA 聚合酶-核酸内切酶-连接酶。

Phaeocystis globosa Virus DNA Polymerase X: a "Swiss Army knife", Multifunctional DNA polymerase-lyase-ligase for Base Excision Repair.

机构信息

Centro de Biología Molecular Severo Ochoa (CSIC-UAM), C/Nicolás Cabrera 1, Campus Cantoblanco, 28049, Madrid, Spain.

Department of Marine Microbiology and Biogeochemistry, NIOZ Royal Netherlands Institute for Sea Research, Utrecht University, NL-1790 AB, Den Burg (Texel), The Netherlands.

出版信息

Sci Rep. 2017 Jul 31;7(1):6907. doi: 10.1038/s41598-017-07378-3.

DOI:10.1038/s41598-017-07378-3
PMID:28761124
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5537341/
Abstract

Phaeocystis globosa virus 16T is a giant virus that belongs to the so-called nucleo-cytoplasmic large DNA virus (NCLDV) group. Its linear dsDNA genome contains an almost full complement of genes required to participate in viral base excision repair (BER). Among them is a gene coding for a bimodular protein consisting of an N-terminal Polβ-like core fused to a C-terminal domain (PgVPolX), which shows homology with NAD-dependent DNA ligases. Analysis of the biochemical features of the purified enzyme revealed that PgVPolX is a multifunctional protein that could act as a "Swiss army knife" enzyme during BER since it is endowed with: 1) a template-directed DNA polymerization activity, preferentially acting on DNA structures containing gaps; 2) 5'-deoxyribose-5-phosphate (dRP) and abasic (AP) site lyase activities; and 3) an NAD-dependent DNA ligase activity. We show how the three activities act in concert to efficiently repair BER intermediates, leading us to suggest that PgVPolX may constitute, together with the viral AP-endonuclease, a BER pathway. This is the first time that this type of protein fusion has been demonstrated to be functional.

摘要

球形棕囊藻病毒 16T 是一种巨型病毒，属于所谓的核质大 DNA 病毒 (NCLDV) 组。其线性 dsDNA 基因组包含几乎完整的一套参与病毒碱基切除修复 (BER) 的基因。其中一个基因编码一种由 N 端 Polβ 样核心融合到 C 端结构域组成的双模蛋白 (PgVPolX)，它与 NAD 依赖性 DNA 连接酶具有同源性。对纯化酶的生化特性分析表明，PgVPolX 是一种多功能蛋白，可作为 BER 过程中的“瑞士军刀”酶，因为它具有：1）模板指导的 DNA 聚合活性，优先作用于含有缺口的 DNA 结构；2）5'-脱氧核糖-5-磷酸 (dRP) 和无碱基 (AP) 位点裂解酶活性；和 3）NAD 依赖性 DNA 连接酶活性。我们展示了这三种活性如何协同作用，有效地修复 BER 中间体，这使我们推测 PgVPolX 可能与病毒 AP 内切酶一起构成 BER 途径。这是首次证明这种类型的蛋白融合具有功能性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/54f9/5537341/f44f1a225a95/41598_2017_7378_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/54f9/5537341/02bf30babf26/41598_2017_7378_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/54f9/5537341/3f8ff593ac43/41598_2017_7378_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/54f9/5537341/a7fe5c7a79a0/41598_2017_7378_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/54f9/5537341/08c54f76576f/41598_2017_7378_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/54f9/5537341/42bd7895cea0/41598_2017_7378_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/54f9/5537341/ce4b86666a4f/41598_2017_7378_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/54f9/5537341/7b99f474cf20/41598_2017_7378_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/54f9/5537341/f44f1a225a95/41598_2017_7378_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/54f9/5537341/02bf30babf26/41598_2017_7378_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/54f9/5537341/3f8ff593ac43/41598_2017_7378_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/54f9/5537341/a7fe5c7a79a0/41598_2017_7378_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/54f9/5537341/08c54f76576f/41598_2017_7378_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/54f9/5537341/42bd7895cea0/41598_2017_7378_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/54f9/5537341/ce4b86666a4f/41598_2017_7378_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/54f9/5537341/7b99f474cf20/41598_2017_7378_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/54f9/5537341/f44f1a225a95/41598_2017_7378_Fig8_HTML.jpg

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