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Title: Methanobactin and the Link between Copper and Bacterial Methane Oxidation

Abstract

Methanobactins (mbs) are low-molecular-mass (<1,200 Da) copper-binding peptides, or chalkophores, produced by many methane-oxidizing bacteria (methanotrophs). These molecules exhibit similarities to certain iron-binding siderophores but are expressed and secreted in response to copper limitation. Structurally, mbs are characterized by a pair of heterocyclic rings with associated thioamide groups that form the copper coordination site. One of the rings is always an oxazolone and the second ring an oxazolone, an imidazolone, or a pyrazinedione moiety. The mb molecule originates from a peptide precursor that undergoes a series of posttranslational modifications, including (i) ring formation, (ii) cleavage of a leader peptide sequence, and (iii) in some cases, addition of a sulfate group. Functionally, mbs represent the extracellular component of a copper acquisition system. Consistent with this role in copper acquisition, mbs have a high affinity for copper ions. Following binding, mbs rapidly reduce Cu 2+ to Cu 1+. In addition to binding copper, mbs will bind most transition metals and near-transition metals and protect the host methanotroph as well as other bacteria from toxic metals. Several other physiological functions have been assigned to mbs, based primarily on their redox and metal-binding properties. Here, we examine the current state of knowledge of thismore » novel type of metal-binding peptide. We also explore its potential applications, how mbs may alter the bioavailability of multiple metals, and the many roles mbs may play in the physiology of methanotrophs.« less

Authors:
 [1];  [2];  [3];  [4];  [5];  [6]
  1. Iowa State Univ., Ames, IA (United States). Roy J. Carver Dept. of Biochemistry, Biophysics and Molecular Biology
  2. Univ. of Michigan, Ann Arbor, MI (United States). Dept. of Civil and Environmental Engineering
  3. Univ. of East Anglia, Norwich (United Kingdom). Earth and Life Systems Alliance and School of Environmental Sciences
  4. Univ. of Wisconsin, Eau Claire, WI (United States). Dept. of Chemistry
  5. Newcastle Univ., Newcastle upon Tyne (United Kingdom). Inst. for Cell and Molecular Biosciences
  6. Univ. of Strasbourg, UMR 7156 UNISTRA-CNRS, (France). Dept. of Microbiology, Genomics and the Environment
Publication Date:
Research Org.:
Univ. of Michigan, Ann Arbor, MI (United States).
Sponsoring Org.:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23; National Science Foundation (NSF); Natural Environment Research Council (NERC); Biotechnology and Biological Sciences Research Council (BBSRC)
OSTI Identifier:
1470738
Grant/Contract Number:  
SC0006630; CHE10112271; NE/F00608X; BB/K008439/1
Resource Type:
Accepted Manuscript
Journal Name:
Microbiology and Molecular Biology Reviews
Additional Journal Information:
Journal Volume: 80; Journal Issue: 2; Journal ID: ISSN 1092-2172
Publisher:
American Society for Microbiology
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY

Citation Formats

DiSpirito, Alan A., Semrau, Jeremy D., Murrell, J. Colin, Gallagher, Warren H., Dennison, Christopher, and Vuilleumier, Stéphane. Methanobactin and the Link between Copper and Bacterial Methane Oxidation. United States: N. p., 2016. Web. doi:10.1128/MMBR.00058-15.
DiSpirito, Alan A., Semrau, Jeremy D., Murrell, J. Colin, Gallagher, Warren H., Dennison, Christopher, & Vuilleumier, Stéphane. Methanobactin and the Link between Copper and Bacterial Methane Oxidation. United States. doi:10.1128/MMBR.00058-15.
DiSpirito, Alan A., Semrau, Jeremy D., Murrell, J. Colin, Gallagher, Warren H., Dennison, Christopher, and Vuilleumier, Stéphane. Wed . "Methanobactin and the Link between Copper and Bacterial Methane Oxidation". United States. doi:10.1128/MMBR.00058-15. https://www.osti.gov/servlets/purl/1470738.
@article{osti_1470738,
title = {Methanobactin and the Link between Copper and Bacterial Methane Oxidation},
author = {DiSpirito, Alan A. and Semrau, Jeremy D. and Murrell, J. Colin and Gallagher, Warren H. and Dennison, Christopher and Vuilleumier, Stéphane},
abstractNote = {Methanobactins (mbs) are low-molecular-mass (<1,200 Da) copper-binding peptides, or chalkophores, produced by many methane-oxidizing bacteria (methanotrophs). These molecules exhibit similarities to certain iron-binding siderophores but are expressed and secreted in response to copper limitation. Structurally, mbs are characterized by a pair of heterocyclic rings with associated thioamide groups that form the copper coordination site. One of the rings is always an oxazolone and the second ring an oxazolone, an imidazolone, or a pyrazinedione moiety. The mb molecule originates from a peptide precursor that undergoes a series of posttranslational modifications, including (i) ring formation, (ii) cleavage of a leader peptide sequence, and (iii) in some cases, addition of a sulfate group. Functionally, mbs represent the extracellular component of a copper acquisition system. Consistent with this role in copper acquisition, mbs have a high affinity for copper ions. Following binding, mbs rapidly reduce Cu2+ to Cu1+. In addition to binding copper, mbs will bind most transition metals and near-transition metals and protect the host methanotroph as well as other bacteria from toxic metals. Several other physiological functions have been assigned to mbs, based primarily on their redox and metal-binding properties. Here, we examine the current state of knowledge of this novel type of metal-binding peptide. We also explore its potential applications, how mbs may alter the bioavailability of multiple metals, and the many roles mbs may play in the physiology of methanotrophs.},
doi = {10.1128/MMBR.00058-15},
journal = {Microbiology and Molecular Biology Reviews},
number = 2,
volume = 80,
place = {United States},
year = {2016},
month = {3}
}

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