| Title | Genome sequence and functional genomic analysis of the oil-degrading bacterium Oleispira antarctica |
| Abstract | Ubiquitous 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. |
| Source | Nature communications 4 |
| Keywords | Genome sequenceOleispira antarctica |
| Journal | Nature communications |
| Editor | Nature Publishing Group., London, Regno Unito |
| Year | 2013 |
| Type | Articolo in rivista |
| DOI | 10.1038/ncomms3156 |
| Authors | Kube, Michael; Chernikova, Tatyana N.; Al-Ramahi, Yamal; Beloqui, Ana; Lopez-Cortez, Nieves; Guazzaroni, Maria-Eugenia; Heipieper, Hermann J.; Klages, Sven; Kotsyurbenko, Oleg R.; Langer, Ines; Nechitaylo, Taras Y.; Luensdorf, Heinrich; Fernandez, Marisol; Juarez, Silvia; Ciordia, Sergio; Singer, Alexander; Kagan, Olga; Egorova, Olga; Petit, Pierre Alain; Stogios, Peter; Kim, Youngchang; Tchigvintsev, Anatoli; Flick, Robert; Denaro, Renata; Genovese, Maria; Albar, Juan P.; Reva, Oleg N.; Martinez-Gomariz, Montserrat; Tran, Hai; Ferrer, Manuel; Savchenko, Alexei; Yakunin, Alexander F.; Yakimov, Michail M.; Golyshina, Olga V.; Reinhardt, Richard; Golyshin, Peter N. |
| Text | 314559 2013 10.1038/ncomms3156 ISI Web of Science WOS 000323716300026 Genome sequence Oleispira antarctica Genome sequence and functional genomic analysis of the oil degrading bacterium Oleispira antarctica Kube, Michael; Chernikova, Tatyana N.; Al Ramahi, Yamal; Beloqui, Ana; Lopez Cortez, Nieves; Guazzaroni, Maria Eugenia; Heipieper, Hermann J.; Klages, Sven; Kotsyurbenko, Oleg R.; Langer, Ines; Nechitaylo, Taras Y.; Luensdorf, Heinrich; Fernandez, Marisol; Juarez, Silvia; Ciordia, Sergio; Singer, Alexander; Kagan, Olga; Egorova, Olga; Petit, Pierre Alain; Stogios, Peter; Kim, Youngchang; Tchigvintsev, Anatoli; Flick, Robert; Denaro, Renata; Genovese, Maria; Albar, Juan P.; Reva, Oleg N.; Martinez Gomariz, Montserrat; Tran, Hai; Ferrer, Manuel; Savchenko, Alexei; Yakunin, Alexander F.; Yakimov, Michail M.; Golyshina, Olga V.; Reinhardt, Richard; Golyshin, Peter N. Max Planck Society; Humboldt University of Berlin; Helmholtz Association; Bangor University; Consejo Superior de Investigaciones Cientificas CSIC ; Universidade de Sao Paulo; Helmholtz Association; Consejo Superior de Investigaciones Cientificas CSIC ; University of Toronto; Argonne National Laboratory; University of Toronto; Argonne National Laboratory; Consiglio Nazionale delle Ricerche CNR ; University of Pretoria; UCM Complutense Univ Ubiquitous 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. 4 Published version Articolo in rivista Nature Publishing Group. 2041 1723 Nature communications Nature communications Nature communications mikhail.iakimov IAKIMOV MIKHAIL renata.denaro DENARO RENATA maria.genovese GENOVESE MARIA |
