TRASH, a novel metal binding domain predicted to be involved in heavy metal sensing, trafficking and resistance

T.J.G. Ettema; M. Huynen; W.M. de Vos; J. van der Oost

doi:10.1016/S0968-0004(03)00037-9

TRASH, a novel metal binding domain predicted to be involved in heavy metal sensing, trafficking and resistance

T.J.G. Ettema, M. Huynen, W.M. de Vos, J. van der Oost

Research output: Contribution to journal › Article › Academic › peer-review

58 Citations (Scopus)

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.

Original language	English
Pages (from-to)	170-173
Journal	Trends in Biochemical Sciences
Volume	28
Issue number	4
DOIs	https://doi.org/10.1016/S0968-0004(03)00037-9
Publication status	Published - 2003

Keywords

copper chaperones
disease proteins
metallochaperone
database
atpases

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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.",

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AU - Ettema, T.J.G.

AU - Huynen, M.

AU - de Vos, W.M.

AU - van der Oost, J.

PY - 2003

Y1 - 2003

N2 - 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.

AB - 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.

KW - copper chaperones

KW - disease proteins

KW - metallochaperone

KW - database

KW - atpases

U2 - 10.1016/S0968-0004(03)00037-9

DO - 10.1016/S0968-0004(03)00037-9

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SP - 170

EP - 173

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

SN - 0968-0004

IS - 4

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