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      Manipulating nitrogen regulation in diazotrophic bacteria for agronomic benefit

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          Abstract

          Biological nitrogen fixation (BNF) is controlled by intricate regulatory mechanisms to ensure that fixed nitrogen is readily assimilated into biomass and not released to the environment. Understanding the complex regulatory circuits that couple nitrogen fixation to ammonium assimilation is a prerequisite for engineering diazotrophic strains that can potentially supply fixed nitrogen to non-legume crops. In this review, we explore how the current knowledge of nitrogen metabolism and BNF regulation may allow strategies for genetic manipulation of diazotrophs for ammonia excretion and provide a contribution towards solving the nitrogen crisis.

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          An Earth-system perspective of the global nitrogen cycle.

          Nicolas Gruber, James N. Galloway (2008)
          Article 0 comments Cited 796 times – based on 0 reviews     Review now
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            Nitrogen assimilation and global regulation in Escherichia coli.

            Larry Reitzer (2002)
            Nitrogen limitation in Escherichia coli controls the expression of about 100 genes of the nitrogen regulated (Ntr) response, including the ammonia-assimilating glutamine synthetase. Low intracellular glutamine controls the Ntr response through several regulators, whose activities are modulated by a variety of metabolites. Ntr proteins assimilate ammonia, scavenge nitrogen-containing compounds, and appear to integrate ammonia assimilation with other aspects of metabolism, such as polyamine metabolism and glutamate synthesis. The leucine-responsive regulatory protein (Lrp) controls the synthesis of glutamate synthase, which controls the Ntr response, presumably through its effect on intracellular glutamine. Some Ntr proteins inhibit the expression of some Lrp-activated genes. Guanosine tetraphosphate appears to control Lrp synthesis. In summary, a network of interacting global regulators that senses different aspects of metabolism integrates nitrogen assimilation with other metabolic processes.
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              Mechanism of Mo-dependent nitrogenase.

              Lance C Seefeldt, Brian M Hoffman, Dennis R Dean (2009)
              Nitrogen-fixing bacteria catalyze the reduction of dinitrogen (N(2)) to two ammonia molecules (NH(3)), the major contribution of fixed nitrogen to the biogeochemical nitrogen cycle. The most widely studied nitrogenase is the molybdenum (Mo)-dependent enzyme. The reduction of N(2) by this enzyme involves the transient interaction of two component proteins, designated the iron (Fe) protein and the MoFe protein, and minimally requires 16 magnesium ATP (MgATP), eight protons, and eight electrons. The current state of knowledge on how these proteins and small molecules together effect the reduction of N(2) to ammonia is reviewed. Included is a summary of the roles of the Fe protein and MgATP hydrolysis, information on the roles of the two metal clusters contained in the MoFe protein in catalysis, insights gained from recent success in trapping substrates and inhibitors at the active-site metal cluster FeMo cofactor, and finally, considerations of the mechanism of N(2) reduction catalyzed by nitrogenase.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Biochem Soc Trans
                Journal ID (iso-abbrev): Biochem. Soc. Trans
                Journal ID (hwp): ppbiost
                Journal ID (publisher-id): BST
                Title: Biochemical Society Transactions
                Publisher: Portland Press Ltd.
                ISSN (Print): 0300-5127
                ISSN (Electronic): 1470-8752
                Publication date (Print): 30 April 2019
                Publication date (Electronic): 1 April 2019
                Volume: 47
                Issue: 2
                Pages: 603-614
                Affiliations
                Department of Molecular Microbiology, John Innes Centre, Colney Lane, Norwich NR4 7UH, U.K.
                Author notes
                Correspondence: Marcelo Bueno Batista ( marcelo.batista@ 123456jic.ac.uk )
                Author information
                http://orcid.org/0000-0002-6642-6624
                https://orcid.org/0000-0002-6348-639X
                Article
                Publisher ID: BST-47-603
                DOI: 10.1042/BST20180342
                PMC ID: 6490700
                PubMed ID: 30936245
                SO-VID: e13d9488-7c18-4d32-a8d9-2cd65177a032
                Copyright © © 2019 The Author(s)
                License:

                This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY).

                History
                Date received : 4 February 2019
                Date revision received : 5 March 2019
                Date accepted : 6 March 2019
                Categories
                Subject: Review Articles
                Subject: Review Article
                Subject: 34
                Subject: 3
                Subject: 10
                Subject: 13
                Subject: 54

                ScienceOpen disciplines: Biochemistry
                Keywords: ammonia excretion,nitrogen fixation,nitrogen regulation,pii signal transduction proteins
                Data availability:
                ScienceOpen disciplines: Biochemistry
                Keywords: ammonia excretion, nitrogen fixation, nitrogen regulation, pii signal transduction proteins

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