A novel mercuric reductase from the unique deep brine environment of atlantis II in the red sea

Handle URI:
http://hdl.handle.net/10754/563106
Title:
A novel mercuric reductase from the unique deep brine environment of atlantis II in the red sea
Authors:
Sayed, Ahmed Anazadeh; Ghazy, Mohamed A.; Ferreira, Ari José Scattone; Setúbal, João Carlos; Chambergo, Felipe Santiago; Ouf, Amged; Adel, Mustafa; Dawe, Adam Sean; Archer, John A.C. ( 0000-0002-3302-3933 ) ; Bajic, Vladimir B. ( 0000-0001-5435-4750 ) ; Siam, Rania; El-Dorry, Hamza A A
Abstract:
Aunique combination of physicochemical conditions prevails in the lower convective layer (LCL) of the brine pool at Atlantis II (ATII) Deep in the Red Sea. With a maximum depth of over 2000 m, the pool is characterized by acidic pH (5.3), high temperature (68 °C), salinity (26%), low light levels, anoxia, and high concentrations of heavy metals. We have established a metagenomic dataset derived from the microbial community in the LCL, and here we describe a gene for a novel mercuric reductase, a key component of the bacterial detoxification system for mercuric and organomercurial species. The metagenome-derived gene and an ortholog from an uncultured soil bacterium were synthesized and expressed in Escherichia coli. The properties of their products show that, in contrast to the soil enzyme, the ATII-LCL mercuric reductase is functional in high salt, stable at high temperatures, resistant to high concentrations of Hg2+, and efficiently detoxifies Hg2+ in vivo. Interestingly, despite the marked functional differences between the orthologs, their amino acid sequences differ by less than 10%. Site-directed mutagenesis and kinetic analysis of the mutant enzymes, in conjunction with three-dimensional modeling, have identified distinct structural features that contribute to extreme halophilicity, thermostability, and high detoxification capacity, suggesting that these were acquired independently during the evolution of this enzyme. Thus, our work provides fundamental structural insights into a novel protein that has undergone multiple biochemical and biophysical adaptations to promote the survival of microorganisms that reside in the extremely demanding environment of the ATII-LCL. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
KAUST Department:
Computational Bioscience Research Center (CBRC); Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division; Applied Mathematics and Computational Science Program
Publisher:
American Society for Biochemistry & Molecular Biology (ASBMB)
Journal:
Journal of Biological Chemistry
Issue Date:
26-Nov-2013
DOI:
10.1074/jbc.M113.493429
PubMed ID:
24280218
PubMed Central ID:
PMC3894346
Type:
Article
ISSN:
00219258
Additional Links:
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3894346
Appears in Collections:
Articles; Applied Mathematics and Computational Science Program; Computational Bioscience Research Center (CBRC); Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorSayed, Ahmed Anazadehen
dc.contributor.authorGhazy, Mohamed A.en
dc.contributor.authorFerreira, Ari José Scattoneen
dc.contributor.authorSetúbal, João Carlosen
dc.contributor.authorChambergo, Felipe Santiagoen
dc.contributor.authorOuf, Amgeden
dc.contributor.authorAdel, Mustafaen
dc.contributor.authorDawe, Adam Seanen
dc.contributor.authorArcher, John A.C.en
dc.contributor.authorBajic, Vladimir B.en
dc.contributor.authorSiam, Raniaen
dc.contributor.authorEl-Dorry, Hamza A Aen
dc.date.accessioned2015-08-03T11:35:55Zen
dc.date.available2015-08-03T11:35:55Zen
dc.date.issued2013-11-26en
dc.identifier.issn00219258en
dc.identifier.pmid24280218en
dc.identifier.doi10.1074/jbc.M113.493429en
dc.identifier.urihttp://hdl.handle.net/10754/563106en
dc.description.abstractAunique combination of physicochemical conditions prevails in the lower convective layer (LCL) of the brine pool at Atlantis II (ATII) Deep in the Red Sea. With a maximum depth of over 2000 m, the pool is characterized by acidic pH (5.3), high temperature (68 °C), salinity (26%), low light levels, anoxia, and high concentrations of heavy metals. We have established a metagenomic dataset derived from the microbial community in the LCL, and here we describe a gene for a novel mercuric reductase, a key component of the bacterial detoxification system for mercuric and organomercurial species. The metagenome-derived gene and an ortholog from an uncultured soil bacterium were synthesized and expressed in Escherichia coli. The properties of their products show that, in contrast to the soil enzyme, the ATII-LCL mercuric reductase is functional in high salt, stable at high temperatures, resistant to high concentrations of Hg2+, and efficiently detoxifies Hg2+ in vivo. Interestingly, despite the marked functional differences between the orthologs, their amino acid sequences differ by less than 10%. Site-directed mutagenesis and kinetic analysis of the mutant enzymes, in conjunction with three-dimensional modeling, have identified distinct structural features that contribute to extreme halophilicity, thermostability, and high detoxification capacity, suggesting that these were acquired independently during the evolution of this enzyme. Thus, our work provides fundamental structural insights into a novel protein that has undergone multiple biochemical and biophysical adaptations to promote the survival of microorganisms that reside in the extremely demanding environment of the ATII-LCL. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.en
dc.publisherAmerican Society for Biochemistry & Molecular Biology (ASBMB)en
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3894346en
dc.titleA novel mercuric reductase from the unique deep brine environment of atlantis II in the red seaen
dc.typeArticleen
dc.contributor.departmentComputational Bioscience Research Center (CBRC)en
dc.contributor.departmentComputer, Electrical and Mathematical Sciences and Engineering (CEMSE) Divisionen
dc.contributor.departmentApplied Mathematics and Computational Science Programen
dc.identifier.journalJournal of Biological Chemistryen
dc.identifier.pmcidPMC3894346en
dc.contributor.institutionDepartment of Biology and the Science and Technology Research Center, School of Sciences and Engineering, American University in Cairo, AUC Avenue, P. O. Box 74, New Cairo 11835, Egypten
dc.contributor.institutionDepartamento de Bioquímica, Instituto de Química, Universidade de São Paulo, Avenida Prof. Lineu Prestes, 748, São Paulo, SP 05508-000, Brazilen
dc.contributor.institutionEscola de Artes, Ciências e Humanidades, Universidade de São Paulo, Avenida Arlindo Bettio 1000, São Paulo, SP 03828-000, Brazilen
kaust.authorDawe, Adam Seanen
kaust.authorArcher, John A.C.en
kaust.authorBajic, Vladimir B.en

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