A dual functional redox enzyme maturation protein for respiratory and assimilatory nitrate reductases in bacteria

Pinchbeck, Benjamin, Soriano-Laguna, Manuel, Sullivan, Matthew ORCID: https://orcid.org/0000-0003-2276-3132, Luque-Almagro, Victor, Rowley, Gary ORCID: https://orcid.org/0000-0002-5421-4333, Ferguson, Stuart J., Roldan, M. Dolores, Richardson, David ORCID: https://orcid.org/0000-0002-6847-1832 and Gates, Andrew ORCID: https://orcid.org/0000-0002-4594-5038 (2019) A dual functional redox enzyme maturation protein for respiratory and assimilatory nitrate reductases in bacteria. Molecular Microbiology, 111 (6). pp. 1592-1603. ISSN 0950-382X

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Abstract

Nitrate is available to microbes in many environments due to sustained use of inorganic fertilizers on agricultural soils and many bacterial and archaeal lineages have the capacity to express respiratory (Nar) and assimilatory (Nas) nitrate reductases to utilize this abundant respiratory substrate and nutrient for growth. Here we show that in the denitrifying bacterium Paracoccus denitrificans, NarJ serves as a chaperone for both the anaerobic respiratory nitrate reductase (NarG) and the assimilatory nitrate reductase (NasC), the latter of which is active during both aerobic and anaerobic nitrate assimilation. Bioinformatic analysis suggests that the potential for this previously unrecognized role for NarJ in functional maturation of other cytoplasmic molybdenum-dependent nitrate reductases may be phylogenetically widespread as many bacteria contain both Nar and Nas systems.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Biological Sciences
UEA Research Groups:	Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Organisms and the Environment Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Medicine and Health Sciences > Research Groups > Pathogen Biology Group
Depositing User:	LivePure Connector
Date Deposited:	11 Mar 2019 13:30
Last Modified:	21 Oct 2024 23:49
URI:	https://ueaeprints.uea.ac.uk/id/eprint/70194
DOI:	10.1111/mmi.14239

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