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.
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| http://dx.doi.org/10.3389/fmicb.2023.1137355 | DOI Listing |
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