Journal
NATURE CHEMICAL BIOLOGY
Volume 4, Issue 10, Pages 609-616Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nchembio.109
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Funding
- US National Institutes of Health [AI 62559]
- William Randolph Hearst Foundation
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [UC1AI062559] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE ON AGING [R01AG025440, R01AG019391, R37AG019391] Funding Source: NIH RePORTER
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A screen of a genomic library from Mycobacterium tuberculosis (Mtb) identified a small, unannotated open reading frame (MT0196) that encodes a 4.9-kDa, cysteine-rich protein. Despite extensive nucleotide divergence, the amino acid sequence is highly conserved among mycobacteria that are pathogenic in vertebrate hosts. We synthesized the protein and found that it preferentially binds up to six Cu(I) ions in a solvent-shielded core. Copper, cadmium and compounds that generate nitric oxide or superoxide induced the gene's expression in Mtb up to 1,000-fold above normal expression. The native protein bound copper within Mtb and partially protected Mtb from copper toxicity. We propose that the product of the MT0196 gene be named mycobacterial metallothionein (MymT). To our knowledge, MymT is the first metallothionein of a Gram-positive bacterium with a demonstrated function.
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