info:eu-repo/semantics/article
Genome Sequence of Azotobacter vinelandii , an Obligate Aerobe Specialized To Support Diverse Anaerobic Metabolic Processes
Fecha
2009-07-15Registro en:
Setubal, João C.; Dos Santos, Patricia Carolina; Goldman, Barry S.; Ertesvag, Helga; Espin, Guadelupe; et al.; Genome Sequence of Azotobacter vinelandii , an Obligate Aerobe Specialized To Support Diverse Anaerobic Metabolic Processes; American Society for Microbiology; Journal of Bacteriology; 191; 14; 15-7-2009; 4534-4545
0021-9193
1098-5530
CONICET Digital
CONICET
Autor
Setubal, João C.
Dos Santos, Patricia Carolina
Goldman, Barry S.
Ertesvag, Helga
Espin, Guadelupe
Rubio, Luis M.
Valla, Svein
Almeida, Nalvo F.
Balasubramanian, Divya
Cromes, Lindsey
Curatti, Leonardo
Du, Zijin
Godsy, Eric
Goodner, Brad
Hellner Burris, Kaitlyn
Hernandez, José A.
Houmiel, Katherine
Imperial, Juan
Kennedy, Christina
Larson, Timothy J.
Latreille, Phil
Ligon, Lauren S.
Lu, Jing
Mærk, Mali
Miller, Nancy M.
Norton, Stacie
O'Carroll, Ina P.
Paulsen, Ian
Raulfs, Estella C.
Roemer, Rebecca
Resumen
Azotobacter vinelandii is a soil bacterium related to the Pseudomonas genus that fixes nitrogen under aerobic conditions while simultaneously protecting nitrogenase from oxygen damage. In response to carbon availability, this organism undergoes a simple differentiation process to form cysts that are resistant to drought and other physical and chemical agents. Here we report the complete genome sequence of A. vinelandii DJ, which has a single circular genome of 5,365,318 bp. In order to reconcile an obligate aerobic lifestyle with exquisitely oxygen-sensitive processes, A. vinelandii is specialized in terms of its complement of respiratory proteins. It is able to produce alginate, a polymer that further protects the organism from excess exogenous oxygen, and it has multiple duplications of alginate modification genes, which may alter alginate composition in response to oxygen availability. The genome analysis identified the chromosomal locations of the genes coding for the three known oxygen-sensitive nitrogenases, as well as genes coding for other oxygen-sensitive enzymes, such as carbon monoxide dehydrogenase and formate dehydrogenase. These findings offer new prospects for the wider application of A. vinelandii as a host for the production and characterization of oxygen-sensitive proteins.