Nitrogen fixation in filamentous cyanobacteria

Haselkorn, Robert; Basche, M.; Böhme, Herbert; Borthakur, Dulal; Borthakur, Pritty B.; Buikema, William J.; Mulligan, Martin E.; Norris, Dominic P.

doi:10.1007/978-1-4684-6432-0_50

Cited by 26 publications

(42 citation statements)

References 15 publications

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“…The diversity of prokaryotic microorganisms with the ability to fix nitrogen is in contrast to the remarkable conservation of the nitrogenase itself (36,58,80).…”

Section: Nitrogenasesmentioning

confidence: 99%

Hydrogenases and Hydrogen Metabolism of Cyanobacteria

Tamagnini

Axelsson

Lindberg

et al. 2002

Microbiol Mol Biol Rev

464

372

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Cyanobacteria may possess several enzymes that are directly involved in dihydrogen metabolism: nitrogenase(s) catalyzing the production of hydrogen concomitantly with the reduction of dinitrogen to ammonia, an uptake hydrogenase (encoded by hupSL) catalyzing the consumption of hydrogen produced by the nitrogenase, and a bidirectional hydrogenase (encoded by hoxFUYH) which has the capacity to both take up and produce hydrogen. This review summarizes our knowledge about cyanobacterial hydrogenases, focusing on recent progress since the first molecular information was published in 1995. It presents the molecular knowledge about cyanobacterial hupSL and hoxFUYH, their corresponding gene products, and their accessory genes before finishing with an applied aspect—the use of cyanobacteria in a biological, renewable production of the future energy carrier molecular hydrogen. In addition to scientific publications, information from three cyanobacterial genomes, the unicellular Synechocystis strain PCC 6803 and the filamentous heterocystous Anabaena strain PCC 7120 and Nostoc punctiforme (PCC 73102/ATCC 29133) is included

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“…The diversity of prokaryotic microorganisms with the ability to fix nitrogen is in contrast to the remarkable conservation of the nitrogenase itself (36,58,80).…”

Section: Nitrogenasesmentioning

confidence: 99%

Hydrogenases and Hydrogen Metabolism of Cyanobacteria

Tamagnini

Axelsson

Lindberg

et al. 2002

Microbiol Mol Biol Rev

464

372

View full text Add to dashboard Cite

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“…Characteristics not uniformly dispersed across taxa or morphologic groups include toxicity (Gleason & Wood, 1987), degradation of xenobiotics (Kuritz & Wolk, 1995), and nitrogen fixation (Haselkorn & Buikema, 1992). In particular, nitrogen fixation is not shared uniformly by any taxonomic or phylogenetic group except the heterocystous cyanobacteria (Young, 1992).…”

Section: Introductionmentioning

confidence: 99%

Homologous regions of the Salmonella enteritidis virulence plasmid and the chromosome of Salmonella typhi encode thiol: disulphide oxidoreductases belonging to the DsbA thioredoxin family

1997

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DNA sequences of a fragment of nifH from diverse cyanobacteria were amplified, cloned and sequenced to determine the evolutionary relationship of nitrogenase within the cyanobacteria as a group, and to provide a basis for the identification of uncultivated strains of cyanobacteria in the environment. Analysis of 30 nitrogenase DNA and deduced amino acid sequences from cyanobacteria representing five major taxonomic subdivisions showed great variation in phylogenetic distances between the sequences. Sequences from heterocystous cyanobacteria formed a coherent cluster, in which branching forms did not form a clade distinct from the non-branching forms. Nitrogenase sequences from the unicellular cyanobacteria GIoeothece and Synechococcus sp. RF-1 formed a cluster, as did sequences from the genera Xenococcus and Myxosarcina. The nifH sequences of filamentous nonheterocystous cyanobacteria were not closely related to each other, forming deep branches with respect to the heterocystous cyanobacterial nifH sequences. The phylogeny of nifH based on amino acid sequences was consistent with taxonomic relationships among the strains; for example, a sequence obtained from a natural assemblage believed to be dominated by 'Lyngbya' clustered with nifH from Lyngbya lagerheimii. Results also indicate that the phylogeny of nifH among the cyanobacteria is largely consistent with the phylogeny of 16s rRNA, and furthermore that the nifH sequence can be used to identify uncultivated strains of nitrogen-f ixing cyanobacteria.

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“…The structural and biochemical modifications of heterocysts contribute to the development of a cellular environment that is conducive to the sustained activity of nitrogenase under oxic growth conditions (19,59). In a cell-free system, nitrogenase is rapidly inactivated in air.…”

mentioning

confidence: 99%

GlbN (cyanoglobin) is a peripheral membrane protein that is restricted to certain Nostoc spp

et al. 1996

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The glbN gene of Nostoc commune UTEX 584 is juxtaposed to nifU and nifH, and it encodes a 12-kDa monomeric hemoglobin that binds oxygen with high affinity. In N. commune UTEX 584, maximum accumulation of GlbN occurred in both the heterocysts and vegetative cells of nitrogen-fixing cultures when the rate of oxygen evolution was repressed to less than 25 mol of O 2 mg of chlorophyll a ؊1 h ؊1 . Accumulation of GlbN coincided with maximum synthesis of NifH and ferredoxin NADP ؉ oxidoreductase (PetH or FNR). A total of 41 strains of cyanobacteria, including 40 nitrogen fixers and representing 16 genera within all five sections of the cyanobacteria were screened for the presence of glbN or GlbN. glbN was present in five Nostoc strains in a single copy. Genomic DNAs from 11 other Nostoc and Anabaena strains, including Anabaena sp. strain PCC 7120, provided no hybridization signals with a glbN probe. A constitutively expressed, 18-kDa protein which cross-reacted strongly with GlbN antibodies was detected in four Anabaena and Nostoc strains and in Trichodesmium thiebautii. The nifU-nifH intergenic region of Nostoc sp. strain MUN 8820 was sequenced (1,229 bp) and was approximately 95% identical to the equivalent region in N. commune UTEX 584. Each strand of the DNA from the nifU-nifH intergenic regions of both strains has the potential to fold into secondary structures in which more than 50% of the bases are internally paired. Mobility shift assays confirmed that NtcA (BifA) bound a site in the nifU-glbN intergenic region of N. commune UTEX 584 approximately 100 bases upstream from the translation initiation site of glbN. This site showed extensive sequence similarity with the promoter region of glnA from Synechococcus sp. strain PCC 7942. In vivo, GlbN had a specific and prominent subcellular location around the periphery of the cytosolic face of the cell membrane, and the protein was found solely in the soluble fraction of cell extracts. Our hypothesis is that GlbN scavenges oxygen for and is a component of a membrane-associated microaerobically induced terminal cytochrome oxidase.

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Nitrogen fixation in filamentous cyanobacteria

Cited by 26 publications

References 15 publications

Hydrogenases and Hydrogen Metabolism of Cyanobacteria

Hydrogenases and Hydrogen Metabolism of Cyanobacteria

Homologous regions of the Salmonella enteritidis virulence plasmid and the chromosome of Salmonella typhi encode thiol: disulphide oxidoreductases belonging to the DsbA thioredoxin family

GlbN (cyanoglobin) is a peripheral membrane protein that is restricted to certain Nostoc spp

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