Programmed DNA rearrangement of a cyanobacterial hupL gene in heterocysts.

Carrasco, Claudio D.; Buettner, Jill A.; Golden, James W.

doi:10.1073/pnas.92.3.791

Cited by 140 publications

(107 citation statements)

References 31 publications

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“…Recently, the uptake hydrogenase genes from Anuhaena 7120 have been shown to undergo rearrangement prior to expression during heterocyst differentiation [21,221. No gene part within the 8.9-kb locus (ORF8, ORF3 or others) shows similarity to the recombinases XisA (involved in nifHDK rearrangement), XisF (for @xiV, or XisC (for hupL) [22], and the consensus sequence for a NtcA-binding site observed upstream of xisA is also not present. Southern blots with different probes of the 8.9-kb segment do not give additional hybridization signals, either from heterocyst or vegetative cell DNA.…”

Section: Resultsmentioning

confidence: 99%

Molecular Biological Analysis of a Bidirectional Hydrogenase from Cyanobacteria

Schmitz

Boison

Hilscher

et al. 1995

European Journal of Biochemistry

145

162

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An 8.9-kb segment with hydrogenase genes from the cyanobacterium Anabaena variabilis has been cloned and sequenced. The sequences show homology to the methyl-viologen-reducing hydrogenases from archaebacteria and, even more striking, to the NAD'-reducing enzymes from Alcaligenes eutrophus and Nocardia opaca as well as to the NADP' -dependent protein from Desulfovibrio fructosovorarzs. The cluster from A. variabilis contains genes coding for both the hydrogenase heterodimer (hoxH and hoxv and for the diaphorase moiety (hoxU and hoxfl described for the A. eurroplius enzyme. In A. variabilis the gene cluster is split by two open reading frames (between hoxY and hoxH and between hoxU and hoxl: respectively), and a probably non-coding 0.9-kb segment in an unusual way. The hoxH partial sequence from Anabaena 71 19 and Anucystis nidulan.7 was amplified by PCR. Using the labeled segment from A. 71 19 as probe, Southern analysis revealed homologous gene segments in the cyanobacteria A. 71 19, Anabaena cylindrica, Arzacystis nidulans and A. variabilis. The bidirectional hydrogenase from A. nidulans was purified and digests were sequenced. The amino acid sequences obtained showed partial identities to the amino acid sequences deduced from the DNA data of the 8.9-kb segment from A. variabilis. Therefore the 8.9-kb segment contains the genes coding for the bidirectional, reversible hydrogenase from cyanobacteria. Crude extracts from A. nidulans perform NAD(P)H-dependent H, evolution corroborating the molecular biological demonstration of the NAD(P)'.-dependent hydrogenase in cyanobacteria.

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Section: Resultsmentioning

confidence: 99%

Molecular Biological Analysis of a Bidirectional Hydrogenase from Cyanobacteria

Schmitz

Boison

Hilscher

et al. 1995

European Journal of Biochemistry

145

162

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“…While the uptake hydrogenase is present in all nitrogenfixing strains tested so far, the bidirectional enzyme is distributed among both nitrogen-fixing and non-nitrogen-fixing cyanobacteria (although it is not a universal cyanobacterial enzyme) (192). The molecular masses indicated for the uptake hydrogenase subunits are mean values calculated from the deduced amino acid sequences of Anabaena strain PCC 7120 (39), Nostoc strain PCC 73102 (150), and A. variabilis ATCC 29413 (79), while the values for the subunits of the bidirectional enzyme are based on data exclusively from A. variabilis ATCC 29413 (173).…”

Section: Nitrogenasesmentioning

confidence: 99%

“…Since the small subunits of all known cyanobacterial uptake hydrogenases lack any N-terminal signal peptide (39,79,150) it has been suggested that the enzyme is localized on the cytoplasmic side of either the cytoplasmic or the thylakoid membrane (13,209). In some filamentous strains, it is particularly expressed in the nitrogen-fixing heterocysts with little or no activity in the photosynthetic vegetative cells (see "Transcription of hupSL" below) (39,87,88,152).…”

Section: Cyanobacterial Uptake Hydrogenasesmentioning

confidence: 99%

Hydrogenases and Hydrogen Metabolism of Cyanobacteria

Tamagnini

Axelsson

Lindberg

et al. 2002

Microbiol Mol Biol Rev

456

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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“…These rearrangements involve the excision of an 11-kb element from nifD (Golden et al, 1988), a 55-kb element from fdxN (Golden et al, 1988), and a 10.5-kb element from hupL (Matveyev et al, 1994 ;Carrasco et al, 1995). These excisions are brought about by three excisases encoded by genes carried on the respective elements : xisA on the 11-kb element (Lammers et al, 1986) ; xisF on the 55-kb element (Carrasco et al, 1994) ; and xisC on the 10.5-kb element (Carrasco et al, 1995). They create the three functional operons nifHDK, nifB-fdxN-nifS-nifU, and hupSL, and leave the three elements as circular DNA molecules with no known function.…”

Section: Heterocyst Developmentmentioning

confidence: 99%