Genome sequence and functional genomic analysis of the oil-degrading bacterium Oleispira antarctica

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. ant...

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Bibliographic Details
Published in:Nature Communications
Main Authors: Kube, Michael, Tatyana N. Chernikova, Yamal Al-Ramahi, Ana Beloqui, Nieves Lopez-Cortez, Maria-Eugenia Guazzaroni, Hermann J. Heipieper, Sven Klages, Oleg R. Kotsyurbenko, Ines Langer, Taras Y. Nechitaylo, Heinrich Lünsdorf, Marisol Fernandez, Silvia Juarez, Sergio Ciordia, Alexander Singer, Olga Kagan, Olga Egorova, Pierre Alain Peti, Peter Stogios, Youngchang Kim, Anatoli Tchigvintsev, Robert Flick, Renata Denaro, Maria Genovese, Juan P. Alba, Oleg N. Reva, Montserrat Martınez-Gomariz, Hai Tran, Manuel Ferrer, Alexei Savchenko, Alexander F. Yakunin, Michail M. Yakimov, Olga V. Golyshina, Richard Reinhardt, Peter N. Golyshin
Format: Article in Journal/Newspaper
Language:unknown
Published: 2013
Subjects:
Antarc*
Antarctica
Online Access:https://zenodo.org/record/13911
https://doi.org/10.1038/ncomms3156
Description
Summary: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.

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