A Design for Life: Prokaryotic metal-binding MerR family regulators

Jonathan Hobman; John Wilkie; Nigel Brown

doi:10.1007/s10534-005-3717-7

A Design for Life: Prokaryotic metal-binding MerR family regulators

Jonathan Hobman, John Wilkie, Nigel Brown

Research output: Contribution to journal › Review article

69 Citations (Scopus)

Abstract

The MerR family of metal-binding, metal-responsive proteins is unique in that they activate transcription from unusual promoters and coordinate metals through cysteine (and in the case of ZntR, histidine) residues. They have conserved primary structures yet can effectively discriminate metals in vivo.

Original language	English
Pages (from-to)	429-36
Number of pages	8
Journal	Biometals
Volume	18
Issue number	4
DOIs	https://doi.org/10.1007/s10534-005-3717-7
Publication status	Published - 1 Aug 2005

Keywords

PbrR
MerR regulators
CueR
ZntR
MerR
cysteine coordination

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10.1007/s10534-005-3717-7

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title = "A Design for Life: Prokaryotic metal-binding MerR family regulators",

abstract = "The MerR family of metal-binding, metal-responsive proteins is unique in that they activate transcription from unusual promoters and coordinate metals through cysteine (and in the case of ZntR, histidine) residues. They have conserved primary structures yet can effectively discriminate metals in vivo.",

keywords = "PbrR, MerR regulators, CueR, ZntR, MerR, cysteine coordination",

author = "Jonathan Hobman and John Wilkie and Nigel Brown",

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AU - Wilkie, John

AU - Brown, Nigel

PY - 2005/8/1

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N2 - The MerR family of metal-binding, metal-responsive proteins is unique in that they activate transcription from unusual promoters and coordinate metals through cysteine (and in the case of ZntR, histidine) residues. They have conserved primary structures yet can effectively discriminate metals in vivo.

AB - The MerR family of metal-binding, metal-responsive proteins is unique in that they activate transcription from unusual promoters and coordinate metals through cysteine (and in the case of ZntR, histidine) residues. They have conserved primary structures yet can effectively discriminate metals in vivo.

KW - PbrR

KW - MerR regulators

KW - CueR

KW - ZntR

KW - MerR

KW - cysteine coordination

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DO - 10.1007/s10534-005-3717-7

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SP - 429

EP - 436

JO - Biometals

JF - Biometals

IS - 4

ER -

A Design for Life: Prokaryotic metal-binding MerR family regulators

Abstract

Keywords

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