A novel covalent modification of nitrogenase in a cyanobacterium

Gallon, John; Cheng, Jiujun; Dougherty, Lisa J; Gallon, Victoria A.; Hilz, Helmuth; Pederson, Dennis M.; Richards, Helen; Rüggeberg, Sabrina; Smith, Christopher J.

doi:10.1016/s0014-5793(00)01229-1

Cited by 14 publications

(14 citation statements)

References 32 publications

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“…Nitrogenase concentrations in populations are rarely quantified, and even when they are, the active and inactive forms of this enzyme complex are not easily distinguished from each other (12,22,54). Furthermore, the number of N 2 -fixing cells in a trichome of Trichodesmium is mostly unknown.…”

Section: Discussionmentioning

confidence: 99%

Modeling the Dynamic Regulation of Nitrogen Fixation in the Cyanobacterium Trichodesmium sp

Rabouille

Staal

Stal

et al. 2006

Appl Environ Microbiol

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Section: Discussionmentioning

confidence: 99%

Modeling the Dynamic Regulation of Nitrogen Fixation in the Cyanobacterium Trichodesmium sp

Rabouille

Staal

Stal

et al. 2006

Appl Environ Microbiol

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“…Instead, it has recently been reported that modification of the nitrogenase Fe protein in the unicellular cyanobacterium Gloeothece sp. strain ATCC 27152 could operate through palmitoylation of the protein (38).…”

Section: Posttranslational Regulationmentioning

confidence: 99%

Nitrogen Control in Cyanobacteria

2001

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“…However, systematic studies using 32 P in vivo labelling and anti-ADP-ribose antibodies showed that the larger NifH band is not ADP-ribosylated in Anabaena variabilis or Gloeothece (Durner et al, 1994;Gallon et al, 2000). Furthermore, draT orthologues have not been found in any cyanobacteria to date.…”

Section: Nitrogenase Post-translational Modification In Cyanobacteriamentioning

confidence: 98%

PII signal transduction proteins: pivotal players in post-translational control of nitrogenase activity

Huergo¹,

Pedrosa²,

Müller-Santos³

et al. 2012

Microbiology

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The fixation of atmospheric nitrogen by the prokaryotic enzyme nitrogenase is an energyexpensive process and consequently it is tightly regulated at a variety of levels. In many diazotrophs this includes post-translational regulation of the enzyme's activity, which has been reported in both bacteria and archaea. The best understood response is the short-term inactivation of nitrogenase in response to a transient rise in ammonium levels in the environment. A number of proteobacteria species effect this regulation through reversible ADP-ribosylation of the enzyme, but other prokaryotes have evolved different mechanisms. Here we review current knowledge of post-translational control of nitrogenase and show that, for the response to ammonium, the P II signal transduction proteins act as key players. IntroductionBiological nitrogen fixation, the reduction of atmospheric N 2 to NH 3 by nitrogen-fixing bacteria, is a key step in the nitrogen cycle. This process is catalysed by nitrogenase, the most common form of which is the molybdenum nitrogenase, composed of dinitrogenase (MoFe protein or NifDK), an a 2 b 2 tetramer encoded by the nifD and nifK genes, respectively, and dinitrogenase reductase (Fe protein or NifH), a c 2 homodimer encoded by the nifH gene. The NifH protein is responsible for ATP-hydrolysisdriven electron transport to the NifDK protein, which contains the site for the reduction of dinitrogen to ammonium (Seefeldt et al., 2009). The reduction of N 2 to two molecules of ammonium is an energy-expensive process requiring the hydrolysis of 16 ATPs.To avoid energy wastage, diazotrophs have evolved both transcriptional and post-translational mechanisms to shut-down nitrogen fixation when ammonium is available in the environment. Post-translational control of nitrogenase activity has been found in a range of diazotrophs and affords a rapid and reversible mechanism by which the organism can respond to transient changes in the environment. Here we review current knowledge of the different mechanisms of post-translational control of nitrogenase. We focus on the two best-described systems: ADP-ribosylation of NifH, which occurs in proteobacteria, and the interaction of NifI regulatory proteins with NifDK in archaea, which potentially also operates in some anaerobic diazotrophic bacteria. Regulation of nitrogenase activity by reversible ADP-ribosylation Historical perspectiveThe process of metabolic inactivation of nitrogenase in response to ammonium was first described in Azotobacter vinelandii (Burris & Wilson, 1946); this phenomenon was later identified in other prokaryotes and named nitrogenase 'switch-off' (Zumft & Castillo, 1978). Different mechanisms are used to regulate nitrogenase post-translationally depending on the organism. The best-studied mechanism operates through reversible ADP-ribosylation of NifH (reviewed by Nordlund, 2000). This system responds to not only the presence of ammonium but also a decrease in the availability of cellular energy, in response to either darkness in phototrophs such as ...

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A novel covalent modification of nitrogenase in a cyanobacterium

Cited by 14 publications

References 32 publications

Modeling the Dynamic Regulation of Nitrogen Fixation in the Cyanobacterium Trichodesmium sp

Modeling the Dynamic Regulation of Nitrogen Fixation in the Cyanobacterium Trichodesmium sp

Nitrogen Control in Cyanobacteria

PII signal transduction proteins: pivotal players in post-translational control of nitrogenase activity

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