Identification of a copper-binding metallothionein in pathogenic mycobacteria Academic Article uri icon

Overview

MeSH Major

  • Copper
  • Metallothionein
  • Mycobacterium tuberculosis

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.

publication date

  • October 2008

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC2749609

Digital Object Identifier (DOI)

  • 10.1038/nchembio.109

PubMed ID

  • 18724363

Additional Document Info

start page

  • 609

end page

  • 16

volume

  • 4

number

  • 10