Sequence and analysis of a plasmid-encoded mercury resistance operon from Mycobacterium marinum identifies MerH, a new mercuric ion transporter.

Mathieu Schué; Lynn Dover; Gurdyal Besra; Julian Parkhill; Neil Brown

doi:10.1128/JB.01063-08

Sequence and analysis of a plasmid-encoded mercury resistance operon from Mycobacterium marinum identifies MerH, a new mercuric ion transporter.

Mathieu Schué, Lynn Dover, Gurdyal Besra, Julian Parkhill, Neil Brown

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

41 Citations (Scopus)

Abstract

In this study, we report the DNA sequence and biological analysis of a mycobacterial mercury resistance operon encoding a novel Hg2+ transporter. MerH was found to transport mercuric ions in Escherichia coli via a pair of essential cysteine residues but only when coexpressed with the mercuric reductase.

Original language	English
Pages (from-to)	439-444
Journal	Journal of Bacteriology
Volume	191
Issue number	1
DOIs	https://doi.org/10.1128/JB.01063-08
Publication status	Published - Jan 2009

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title = "Sequence and analysis of a plasmid-encoded mercury resistance operon from Mycobacterium marinum identifies MerH, a new mercuric ion transporter.",

abstract = "In this study, we report the DNA sequence and biological analysis of a mycobacterial mercury resistance operon encoding a novel Hg2+ transporter. MerH was found to transport mercuric ions in Escherichia coli via a pair of essential cysteine residues but only when coexpressed with the mercuric reductase.",

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AU - Schué, Mathieu

AU - Dover, Lynn

AU - Besra, Gurdyal

AU - Parkhill, Julian

AU - Brown, Neil

PY - 2009/1

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N2 - In this study, we report the DNA sequence and biological analysis of a mycobacterial mercury resistance operon encoding a novel Hg2+ transporter. MerH was found to transport mercuric ions in Escherichia coli via a pair of essential cysteine residues but only when coexpressed with the mercuric reductase.

AB - In this study, we report the DNA sequence and biological analysis of a mycobacterial mercury resistance operon encoding a novel Hg2+ transporter. MerH was found to transport mercuric ions in Escherichia coli via a pair of essential cysteine residues but only when coexpressed with the mercuric reductase.

UR - https://www.scopus.com/pages/publications/58149479229

U2 - 10.1128/JB.01063-08

DO - 10.1128/JB.01063-08

M3 - Article

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VL - 191

SP - 439

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JO - Journal of Bacteriology

JF - Journal of Bacteriology

IS - 1

ER -

Sequence and analysis of a plasmid-encoded mercury resistance operon from Mycobacterium marinum identifies MerH, a new mercuric ion transporter.

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