title: TRASH: a novel metal-binding domain predicted to be involved in heavy-metal sensing, trafficking and resistance.
abstract: We describe a previously undetected domain - TRASH - containing a well-conserved cysteine motif that we anticipate to be involved in metal coordination. TRASH is encoded by multiple prokaryotic genomes and is present in transcriptional regulators, cation-transporting ATPases and hydrogenases, and is also present as a stand-alone module. The observed domain associations and conserved genome context of TRASH-encoding genes in prokaryotic genomes suggest that TRASH constitutes a novel component in metal trafficking and heavy-metal resistance. The role of the multiple copies of TRASH that are present in vertebrate proteins remains to be elucidated.
authors.affiliation: Laboratory of Microbiology, Wageningen University and Research Center Hesselink van Suchtelenweg 4, NL-6703CT, Wageningen, The Netherlands. thijs.ettema@wur.nl
authors.forename: Thijs J G
authors.initials: TJ
authors.lastname: Ettema
authors.forename: Martijn A
authors.initials: MA
authors.lastname: Huynen
authors.forename: Willem M
authors.initials: WM
authors.lastname: de Vos
authors.forename: John
authors.initials: J
authors.lastname: van der Oost
mesh_terms: D000251:Adenosine Triphosphatases / Q000235:genetics / Q000378:metabolism; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001692:Biological Transport; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism; D006801:Humans; D019216:Metals, Heavy / Q000378:metabolism*; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment
chemical_list: D004268:DNA-Binding Proteins; D019216:Metals, Heavy; D018832:Molecular Chaperones; D000251:Adenosine Triphosphatases