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The role of a 2-on-2 haemoglobin in oxidative and nitrosative stress resistance of Antarctic Pseudoalteromonas haloplanktis TAC125
Authors:Ermenegilda Parrilli  Maria Giuliani  Daniela Giordano  Roberta Russo  Gennaro Marino  Cinzia Verde  Maria Luisa Tutino
Affiliation:1. Dipartimento di Chimica Organica e Biochimica, Università di Napoli Federico II – Complesso Universitario M.S. Angelo, via Cinthia 4, 80126 Naples, Italy;2. Facoltà di Scienze Biotecnologiche Università di Napoli Federico II, Naples, Italy;3. Institute of Protein Biochemistry (IBP), National Research Council (CNR), Via Pietro Castellino 111, I-80131 Naples, Italy
Abstract:The 2-on-2 haemoglobins, previously named truncated, are monomeric, low-molecular weight oxygen-binding proteins that share the overall topology with vertebrate haemoglobins. Although several studies on 2-on-2 haemoglobins have been reported, their physiological and biochemical functions are not yet well defined, and various roles have been suggested. The genome of the psychrophilic Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125 (PhTAC125) is endowed with three genes encoding 2-on-2 haemoglobins. To investigate the function played by one of the three trHbs, PhHbO, a PhTAC125 genomic mutant strain was constructed, in which the encoding gene was knocked-out. The mutant strain was grown under controlled conditions and several aspects of bacterium physiology were compared with those of wild-type cells when dissolved oxygen pressure in solution and growth temperature were changed. Interestingly, inactivation of the PhHbO encoding gene makes the mutant bacterial strain sensitive to high solution oxygen pressure, to H2O2, and to a nitrosating agent, suggesting the involvement of PhHbO in oxidative and nitrosative stress resistance.
Keywords:Pseudoalteromonas haloplanktis TAC125   Cold-adapted bacteria   Truncated haemoglobin   Oxygen scavenger
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