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. 1997 Dec;179(23):7587-90.
doi: 10.1128/jb.179.23.7587-7590.1997.

Role of NifS in maturation of glutamine phosphoribosylpyrophosphate amidotransferase

S Chen  1 , L Zheng, D R Dean, H Zalkin
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Role of NifS in maturation of glutamine phosphoribosylpyrophosphate amidotransferase

S Chen et al. J Bacteriol. 1997 Dec.

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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