PMID:22196016
| Citation |
Hensley, MP, Gunasekera, TS, Easton, JA, Sigdel, TK, Sugarbaker, SA, Klingbeil, L, Breece, RM, Tierney, DL and Crowder, MW (2012) Characterization of Zn(II)-responsive ribosomal proteins YkgM and L31 in E. coli. J. Inorg. Biochem. 111:164-72 |
|---|---|
| Abstract |
RT-PCR and DNA microarrays were used to probe for Zn(II)-responsive genes in E. coli cells that were made Zn(II) deficient. Microarray data revealed 114 genes were significantly up-regulated and 146 genes were significantly down-regulated in Zn(II) deficient conditions. The three most up-regulated genes were (1) znuA, which encodes for a periplasmic protein known to be involved with Zn(II) import, (2) yodA, which encodes for a periplasmic protein with unknown function, and (3) ykgM, which encodes for a ribosomal protein that is thought to be a paralog of ribosomal protein L31. YodA was over-expressed and purified as a maltose binding protein (MBP) fusion protein and shown to tightly bind 4 equivalents of Zn(II). Metal analyses showed that MBP-YkgM does not bind Zn(II). On the other hand, MBP-L31 tightly binds 1 equivalent of Zn(II). EXAFS studies on MBP-L31 suggest a ligand field of 1 histidine, 1 cysteine, and 2 additional N/O scatterers. Site-directed mutagenesis studies suggest that Cys16 coordinates Zn(II) in MBP-L31 and that the other three cysteines do not bind metal. These results are discussed in light of Zn(II) starvation model that has been postulated for B. subtilis. |
| Links |
PubMed PMC3325339 Online version:10.1016/j.jinorgbio.2011.11.022 |
| Keywords |
ATP-Binding Cassette Transporters/chemistry; ATP-Binding Cassette Transporters/genetics; ATP-Binding Cassette Transporters/metabolism; Cysteine/chemistry; Cysteine/genetics; Cysteine/metabolism; Escherichia coli/drug effects; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Gene Expression Profiling; Gene Expression Regulation, Bacterial/drug effects; Histidine/chemistry; Histidine/genetics; Histidine/metabolism; Models, Molecular; Mutagenesis, Site-Directed; Oligonucleotide Array Sequence Analysis; Protein Binding; Protein Structure, Tertiary; Reverse Transcriptase Polymerase Chain Reaction; Ribosomal Proteins/chemistry; Ribosomal Proteins/genetics; Ribosomal Proteins/metabolism; Time Factors; X-Ray Absorption Spectroscopy/methods; Zinc/metabolism; Zinc/pharmacology |
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