Role of NifS in maturation of glutamine phosphoribosylpyrophosphate amidotransferase.
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.
Chen
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Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907, USA.
Zheng
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Dean
D R
DR
Zalkin
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H
D000582:Amidophosphoribosyltransferase / Q000378:metabolism*; D016948:Azotobacter vinelandii / Q000201:enzymology / Q000235:genetics; D001412:Bacillus subtilis / Q000201:enzymology; D013437:Carbon-Sulfur Lyases; D004792:Enzyme Precursors / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D008190:Lyases / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism
D004792:Enzyme Precursors; D011994:Recombinant Proteins; D000582:Amidophosphoribosyltransferase; D008190:Lyases; D013437:Carbon-Sulfur Lyases; C080546:cysteine desulfurase