Cloning, molecular analysis and insertional mutagenesis of the bidirectional hydrogenase genes from the cyanobacterium <i>Anacystis nidulans</i>

Boison, Gudrun; Schmitz, Oliver; Михеева, Л. Е.; Шестаков, С. В.; Bothe, Hermann

doi:10.1016/0014-5793(96)00936-2

Cited by 62 publications

(35 citation statements)

References 34 publications

(62 reference statements)

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“…Some physiological data, together with analysis of a mutant of the bidirectional hydrogenase gene hoxH, indicate that the unicellular non-nitrogen-fixing Synechococcus strain PCC 6301 (Anacystis nidulans) may also possess a hydrogen uptake enzyme (29,48,(154)(155)(156). However, the presence of an uptake hydrogenase in non-nitrogen-fixing cyanobacteria is still a controversial subject, but the increasing availability of molecular data, particularly from genome projects, will help to clarify this question.…”

Section: Cyanobacterial Uptake Hydrogenasesmentioning

confidence: 99%

“…5). The intergenic distances between hoxF and hoxU in both Synechococcus strain PCC 6301 and Anabaena strain PCC 7120 are longer (at least 16 and approximately 9 kb, respec- (29,30), and Synechocystis PCC 6803 (S. PCC 6803) (12,95,144). Vertical lines correspond to the positions of triplets encoding conserved cysteine residues compared to other microorganisms (for more details, see Table 4).…”

Section: Cyanobacterial Bidirectional Hydrogenasesmentioning

confidence: 99%

“…7). Among the first hyp genes to be identified were hypABF in Synechococcus strain PCC 6301 (29) and hypB in Anabaena strain PCC 7120 (originally published as hupB [70]) (Fig. 7).…”

Section: Accessory Genesmentioning

confidence: 99%

“…The histidine-rich N terminals of hypB are indicated (1). Anabaena strain PCC 7120 (A. PCC 7120) (70, 71; http://www.kazusa.or.jpn /cyano/anabaena), Nostoc PCC 73102 (N. PCC 73102) (74; http://www.jgi.doe.gov/JGI_microbial/html/nostoc/nostoc_homepage/html); Synechococcus strain PCC 7002 (S. PCC 7002) (171), Synechococcus strain PCC 6301 (S. PCC 6301) (29), and Synechocystis strain PCC 6803 (S. PCC 6803) (95,144). (171) slr1675 (95,144) sll1078 (95,144) Sll1432 (95,144) sll1079 (95,144) ssl3580 (95,144) slr1498 (95,144) sll1462 (95,144) sll0322 (95,144) c286, AF006594 (71) drogen.…”

Section: Strategies For Improving Cyanobacterial Strains For Photobiomentioning

confidence: 99%

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Hydrogenases and Hydrogen Metabolism of Cyanobacteria

Tamagnini

Axelsson

Lindberg

et al. 2002

Microbiol Mol Biol Rev

455

369

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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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Section: Cyanobacterial Uptake Hydrogenasesmentioning

confidence: 99%

Section: Cyanobacterial Bidirectional Hydrogenasesmentioning

confidence: 99%

“…7). Among the first hyp genes to be identified were hypABF in Synechococcus strain PCC 6301 (29) and hypB in Anabaena strain PCC 7120 (originally published as hupB [70]) (Fig. 7).…”

Section: Accessory Genesmentioning

confidence: 99%

Section: Strategies For Improving Cyanobacterial Strains For Photobiomentioning

confidence: 99%

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Hydrogenases and Hydrogen Metabolism of Cyanobacteria

Tamagnini

Axelsson

Lindberg

et al. 2002

Microbiol Mol Biol Rev

455

369

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“…In addition, a bi-directional enzyme (encoded by hoxEFUYH) may be present which, depending on the growth conditions, may display the capacity of both producing and consuming H 2 (Lambert & Smith, 1981;Houchins, 1984;Schmitz et al, 2002;Tamagnini et al, 2002). All cyanobacteria examined so far contain an uptake, a bi-directional or both the hydrogenases (Schmitz et al, 1995(Schmitz et al, , 2002Boison et al, 1996;Tamagnini et al, 2000Tamagnini et al, , 2002Sheremetieva et al, 2002; Schütz et al, 2004). Moreover, the uptake-type enzyme has been found in all nitrogen fixing cyanobacterial strains studied to date (Carrasco & Golden, 1995;Oxelfelt et al, 1998;Happe et al, 2000;Tamagnini et al, 2000Tamagnini et al, , 2002 Schütz et al, 2004).…”

mentioning

confidence: 99%

Characterization and transcriptional analysis of hupSLW in Gloeothece sp. ATCC 27152: an uptake hydrogenase from a unicellular cyanobacterium

et al. 2004

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The structural genes (hupSL) encoding an uptake hydrogenase in the unicellular cyanobacterium Gloeothece sp. ATCC 27152, a strain capable of aerobic N 2 fixation, were identified and sequenced. 39-RACE experiments uncovered the presence of an additional ORF 184 bp downstream of hupL, showing a high degree of sequence identity with a gene encoding an uptake-hydrogenase-specific endopeptidase (hupW ) in other cyanobacteria. In addition, the transcription start point was identified 238 bp upstream of the hupS translational start. RT-PCR experiments revealed that hupW is co-transcribed with the uptake hydrogenase structural genes in Gloeothece sp. ATCC 27152. In addition, Northern hybridizations clearly showed that hupSLW are transcribed under nitrogen fixing conditions, but not in the presence of combined nitrogen. A putative NtcA binding site was identified in the promoter region upstream of hupS, centred at "41?5 bp with respect to the transcription start point. Electrophoretic retardation of a labelled DNA fragment (harbouring the putative NtcA-binding motif) was significantly affected by an Escherichia coli cell-free extract containing overexpressed NtcA, suggesting that NtcA is involved in the transcriptional regulation of hupSLW. INTRODUCTIONSeveral species of bacteria and cyanobacteria are capable of N 2 fixation. During the N 2 fixation process H 2 is formed as a by-product. This nitrogenase-dependent H 2 production is often compromised by the presence of an uptake hydrogenase (encoded by hupSL) that rapidly consumes the H 2 generated. In addition, a bi-directional enzyme (encoded by hoxEFUYH) may be present which, depending on the growth conditions, may display the capacity of both producing and consuming H 2 (Lambert & Smith, 1981;Houchins, 1984;Schmitz et al., 2002;Tamagnini et al., 2002). All cyanobacteria examined so far contain an uptake, a bi-directional or both the hydrogenases (Schmitz et al., 1995(Schmitz et al., , 2002Boison et al., 1996;Tamagnini et al., 2000Tamagnini et al., , 2002Sheremetieva et al., 2002; Schütz et al., 2004). Moreover, the uptake-type enzyme has been found in all nitrogen fixing cyanobacterial strains studied to date (Carrasco & Golden, 1995;Oxelfelt et al., 1998;Happe et al., 2000;Tamagnini et al., 2000Tamagnini et al., , 2002 Schütz et al., 2004).The first data on cyanobacterial hupSL transcription appeared in 1995 (Carrasco & Golden, 1995). RT-PCR experiments on Anabaena/Nostoc sp. strain PCC 7120 demonstrated that hupL transcription coincides with the formation of heterocysts. Subsequent studies, in other filamentous strains, have confirmed the induction of an hupL transcript under nitrogen-fixing conditions only (Axelsson et al., 1999;Happe et al., 2000; Hansel et al., 2001). One exception is Anabaena variabilis ATCC 29413, where a low level of hupL expression has been detected in vegetative cells grown with the addition of ammonia (Boison et al., 2000). In all the cyanobacterial strains 3Present address: Department of Physiological Botany, Evolutionary Biology Centre,...

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