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dc.contributor.authorKube, Michael
dc.contributor.authorChernikova, Tatyana N
dc.contributor.authorAl-Ramahi, Yamal
dc.contributor.authorBeloqui, Ana
dc.contributor.authorLopez-Cortez, Nieves
dc.contributor.authorGuazzaroni, María-Eugenia
dc.contributor.authorHeipieper, Hermann J
dc.contributor.authorKlages, Sven
dc.contributor.authorKotsyurbenko, Oleg R
dc.contributor.authorLanger, Ines
dc.contributor.authorNechitaylo, Taras Y
dc.contributor.authorLünsdorf, Heinrich
dc.contributor.authorFernández, Marisol
dc.contributor.authorJuárez, Silvia
dc.contributor.authorCiordia, Sergio
dc.contributor.authorSinger, Alexander
dc.contributor.authorKagan, Olga
dc.contributor.authorEgorova, Olga
dc.contributor.authorAlain Petit, Pierre
dc.contributor.authorStogios, Peter
dc.contributor.authorKim, Youngchang
dc.contributor.authorTchigvintsev, Anatoli
dc.contributor.authorFlick, Robert
dc.contributor.authorDenaro, Renata
dc.contributor.authorGenovese, Maria
dc.contributor.authorAlbar, Juan P
dc.contributor.authorReva, Oleg N
dc.contributor.authorMartínez-Gomariz, Montserrat
dc.contributor.authorTran, Hai
dc.contributor.authorFerrer, Manuel
dc.contributor.authorSavchenko, Alexei
dc.contributor.authorYakunin, Alexander F
dc.contributor.authorYakimov, Michail M
dc.contributor.authorGolyshina, Olga V
dc.contributor.authorReinhardt, Richard
dc.contributor.authorGolyshin, Peter N
dc.date.accessioned2013-08-22T14:07:55Z
dc.date.available2013-08-22T14:07:55Z
dc.date.issued2013-07-23
dc.identifier.citationGenome sequence and functional genomic analysis of the oil-degrading bacterium Oleispira antarctica. 2013, 4:2156 Nat Communen_GB
dc.identifier.issn2041-1723
dc.identifier.pmid23877221
dc.identifier.doi10.1038/ncomms3156
dc.identifier.urihttp://hdl.handle.net/10033/299523
dc.description.abstractUbiquitous bacteria from the genus Oleispira drive oil degradation in the largest environment on Earth, the cold and deep sea. Here we report the genome sequence of Oleispira antarctica and show that compared with Alcanivorax borkumensis-the paradigm of mesophilic hydrocarbonoclastic bacteria-O. antarctica has a larger genome that has witnessed massive gene-transfer events. We identify an array of alkane monooxygenases, osmoprotectants, siderophores and micronutrient-scavenging pathways. We also show that at low temperatures, the main protein-folding machine Cpn60 functions as a single heptameric barrel that uses larger proteins as substrates compared with the classical double-barrel structure observed at higher temperatures. With 11 protein crystal structures, we further report the largest set of structures from one psychrotolerant organism. The most common structural feature is an increased content of surface-exposed negatively charged residues compared to their mesophilic counterparts. Our findings are relevant in the context of microbial cold-adaptation mechanisms and the development of strategies for oil-spill mitigation in cold environments.
dc.language.isoenen
dc.rightsArchived with thanks to Nature communicationsen_GB
dc.titleGenome sequence and functional genomic analysis of the oil-degrading bacterium Oleispira antarctica.en
dc.typeArticleen
dc.contributor.department1] Max-Planck Institute for Molecular Genetics, Berlin-Dahlem D-14195, Germany [2] Section Phytomedicine, Department of Crop and Animal Sciences, Humboldt-Universität zu Berlin, Berlin-Dahlem D-14195, Germany.en_GB
dc.identifier.journalNature communicationsen_GB
refterms.dateFOA2018-06-12T22:25:38Z
html.description.abstractUbiquitous bacteria from the genus Oleispira drive oil degradation in the largest environment on Earth, the cold and deep sea. Here we report the genome sequence of Oleispira antarctica and show that compared with Alcanivorax borkumensis-the paradigm of mesophilic hydrocarbonoclastic bacteria-O. antarctica has a larger genome that has witnessed massive gene-transfer events. We identify an array of alkane monooxygenases, osmoprotectants, siderophores and micronutrient-scavenging pathways. We also show that at low temperatures, the main protein-folding machine Cpn60 functions as a single heptameric barrel that uses larger proteins as substrates compared with the classical double-barrel structure observed at higher temperatures. With 11 protein crystal structures, we further report the largest set of structures from one psychrotolerant organism. The most common structural feature is an increased content of surface-exposed negatively charged residues compared to their mesophilic counterparts. Our findings are relevant in the context of microbial cold-adaptation mechanisms and the development of strategies for oil-spill mitigation in cold environments.


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