通过使用多蛋白策略在[具体环境或生物]中组装固氮酶生物合成途径。 （你提供的原文中“in”后面缺少具体内容）
Assembly of nitrogenase biosynthetic pathway in by using polyprotein strategy.
作者信息
Wang Minyang, Shang Yimin, Liu Xiaomeng, Chen Sanfeng
机构信息
State Key Laboratory for Agrobiotechnology and College of Biological Sciences, China Agricultural University, Beijing, China.
出版信息
Front Microbiol. 2023 Mar 2;14:1137355. doi: 10.3389/fmicb.2023.1137355. eCollection 2023.
Nitrogenase in some bacteria and archaea catalyzes conversion of N to ammonia. To reconstitute a nitrogenase biosynthetic pathway in a eukaryotic host is still a challenge, since synthesis of nitrogenase requires a large number of (trogen ixation) genes. Viral 2A peptide mediated "cleavage" of polyprotein is one of strategies for multigene co-expression. Here, we show that cleavage efficiency of NifB-2A-NifH polyprotein linked by four different 2A peptides (P2A, T2A, E2A, and F2A) in ranges from ~50% to ~90%. The presence of a 2A tail in NifB, NifH, and NifD does not affect their activity. Western blotting shows that 9 Nif proteins (NifB, NifH, NifD, NifK, NifE, NifN, NifX, HesA, and NifV) from that are fused into two polyproteins 2A peptides are co-expressed in . . Expressed NifH from NifU and NifS and . NifH fusion linked 2A in . exhibits Fe protein activity.
一些细菌和古细菌中的固氮酶催化将N转化为氨。在真核宿主中重建固氮酶生物合成途径仍然是一项挑战，因为固氮酶的合成需要大量（固氮）基因。病毒2A肽介导的多聚蛋白“切割”是多基因共表达的策略之一。在这里，我们表明，由四种不同的2A肽（P2A、T2A、E2A和F2A）连接的NifB-2A-NifH多聚蛋白在[具体范围]中的切割效率在约50%至约90%之间。NifB、NifH和NifD中2A尾巴的存在不影响它们的活性。蛋白质免疫印迹显示，来自[具体来源]的9种Nif蛋白（NifB、NifH、NifD、NifK、NifE、NifN、NifX、HesA和NifV）融合到两个带有2A肽的多聚蛋白中在[具体宿主]中共表达。[具体来源]中表达的NifH依赖于NifU和NifS。[具体来源]中由2A连接的NifH融合蛋白表现出铁蛋白活性。
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