The identification of a novel protein involved in molybdenum cofactor biosynthesis in Escherichia coli.

Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE

Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology

Carbon-Sulfur Lyases/*metabolism ; Coenzymes/*biosynthesis ; Escherichia coli/*metabolism ; Escherichia coli Proteins/*metabolism ; Metalloproteins/*biosynthesis ; Sulfurtransferases/*metabolism; Carbon-Sulfur Lyases/genetics ; Coenzymes/genetics ; Escherichia coli/genetics ; Escherichia coli Proteins/genetics ; Humans ; Metalloproteins/genetics ; Molybdenum Cofactors ; Nucleotidyltransferases/genetics ; Nucleotidyltransferases/metabolism ; Pteridines ; Sulfurtransferases/genetics

In the second step of the molybdenum cofactor (Moco) biosynthesis in Escherichia coli, the l-cysteine desulfurase IscS was identified as the primary sulfur donor for the formation of the thiocarboxylate on the small subunit (MoaD) of MPT synthase, which catalyzes the conversion of cyclic pyranopterin monophosphate to molybdopterin (MPT). Although in Moco biosynthesis in humans, the thiocarboxylation of the corresponding MoaD homolog involves two sulfurtransferases, an l-cysteine desulfurase, and a rhodanese-like protein, the rhodanese-like protein in E. coli remained enigmatic so far. Using a reverse approach, we identified a so far unknown sulfurtransferase for the MoeB-MoaD complex by protein-protein interactions. We show that YnjE, a three-domain rhodanese-like protein from E. coli, interacts with MoeB possibly for sulfur transfer to MoaD. The E. coli IscS protein was shown to specifically interact with YnjE for the formation of the persulfide group on YnjE. In a defined in vitro system consisting of MPT synthase, MoeB, Mg-ATP, IscS, and l-cysteine, YnjE was shown to enhance the rate of the conversion of added cyclic pyranopterin monophosphate to MPT. However, YnjE was not an enhancer of the cysteine desulfurase activity of IscS. This is the first report identifying the rhodanese-like protein YnjE as being involved in Moco biosynthesis in E. coli. We believe that the role of YnjE is to make the sulfur transfer from IscS for Moco biosynthesis more specific because IscS is involved in a variety of different sulfur transfer reactions in the cell.

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0 (Coenzymes)
0 (Escherichia coli Proteins)
0 (Metalloproteins)
0 (Molybdenum Cofactors)
0 (Pteridines)
ATN6EG42UQ (molybdenum cofactor)
EC 2.7.7.- (MoeB protein, E coli)
EC 2.7.7.- (Nucleotidyltransferases)
EC 2.8.1.- (Sulfurtransferases)
EC 2.8.1.- (YnjE protein, E coli)
EC 2.8.1.- (molybdopterin synthase)
EC 4.4.- (Carbon-Sulfur Lyases)
EC 4.4.1.- (cysteine desulfurase)

Date Created: 20110823 Date Completed: 20111212 Latest Revision: 20211203

20221213

PMC3195606

10.1074/jbc.M111.282368

21856748