Abstract
Glutamine phosphoribosylpyrophosphate amidotransferase from Bacillus subtilis is synthesized as an inactive precursor that requires two maturation steps: incorporation of a [4Fe-4S] center and cleavage of an 11-residue NH2-terminal propeptide. Overproduction from a multicopy plasmid in Escherichia coli leads to the formation of soluble proenzyme and mature enzyme forms as well as a small fraction of insoluble proenzyme. Heterologous expression of Azotobacter vinelandii nifS from a compatible plasmid increased the maturation of the soluble proenzyme three- to fourfold without influencing the content of the insoluble fraction. These results support a role for NifS in heterologous Fe-S cluster assembly and enzyme maturation.
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Dates
Type | When |
---|---|
Created | 8 years, 9 months ago (Nov. 10, 2016, 11:17 a.m.) |
Deposited | 4 years, 1 month ago (July 29, 2021, 2:07 p.m.) |
Indexed | 4 weeks, 1 day ago (Aug. 5, 2025, 8:42 a.m.) |
Issued | 27 years, 9 months ago (Dec. 1, 1997) |
Published | 27 years, 9 months ago (Dec. 1, 1997) |
Published Print | 27 years, 9 months ago (Dec. 1, 1997) |
@article{Chen_1997, title={Role of NifS in maturation of glutamine phosphoribosylpyrophosphate amidotransferase}, volume={179}, ISSN={1098-5530}, url={http://dx.doi.org/10.1128/jb.179.23.7587-7590.1997}, DOI={10.1128/jb.179.23.7587-7590.1997}, number={23}, journal={Journal of Bacteriology}, publisher={American Society for Microbiology}, author={Chen, S and Zheng, L and Dean, D R and Zalkin, H}, year={1997}, month=dec, pages={7587–7590} }