Article abstract
Nature Chemical Biology 4, 609 - 616 (2008)
Published online: 24 August 2008 | doi:10.1038/nchembio.109
Identification of a copper-binding metallothionein in pathogenic mycobacteria
Ben Gold1, Haiteng Deng2, Ruslana Bryk1, Diana Vargas3, David Eliezer4, Julia Roberts1, Xiuju Jiang1 & Carl Nathan1
Abstract
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.
- Department of Microbiology and Immunology, Weill Cornell Medical College, 1300 York Avenue, New York, New York 10065, USA.
- Proteomics Resource Center, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA.
- Department of Molecular Genetics, Public Health Research Institute, 225 Warren Street, Newark, New Jersey 07103, USA.
- Department of Biochemistry, Weill Cornell Medical College, 1300 York Avenue, New York, New York 10065, USA.
- Program in Immunology and Microbial Pathogenesis and Program in Molecular Biology, Weill Graduate School of Medical Sciences of Cornell University, 1300 York Avenue, New York, New York 10065, USA.
Correspondence to: Carl Nathan1 e-mail: cnathan@med.cornell.edu
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