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J. Bacteriol., 12 1997, 7587-7590, Vol 179, No. 23
Copyright © 1997, American Society for Microbiology

Role of NifS in maturation of glutamine phosphoribosylpyrophosphate amidotransferase

S Chen, L Zheng, DR Dean and H Zalkin
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907, USA.

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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