Quantitative analysis of expression of two circadian clock‐controlled gene clusters coding for the bidirectional hydrogenase in the cyanobacterium <i>Synechococcus</i> sp. PCC7942

Schmitz, Oliver; Boison, Gudrun; Bothe, Hermann

doi:10.1046/j.1365-2958.2001.02612.x

Cited by 30 publications

(36 citation statements)

References 30 publications

(55 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It has been shown that in Synechocystis sp. strain PCC 6803 expression of the hox genes is directed by the circadian rhythms (33). In R. eutropha a hydrogen-sensing signal transduction cascade controls the biosynthesis of the soluble NAD ϩ -reducing hydrogenase (21).…”

Section: Resultsmentioning

confidence: 99%

Cyanobacterial-Type, Heteropentameric, NAD ⁺ -Reducing NiFe Hydrogenase in the Purple Sulfur Photosynthetic Bacterium Thiocapsa roseopersicina

Rákhely

Kovács

Maróti

et al. 2004

Appl Environ Microbiol

View full text Add to dashboard Cite

Structural genes coding for two membrane-associated NiFe hydrogenases in the phototrophic purple sulfur bacterium Thiocapsa roseopersicina (hupSL and hynSL) have recently been isolated and characterized. Deletion of both hydrogenase structural genes did not eliminate hydrogenase activity in the cells, and considerable hydrogenase activity was detected in the soluble fraction. The enzyme responsible for this activity was partially purified, and the gene cluster coding for a cytoplasmic, NAD ؉ -reducing NiFe hydrogenase was identified and sequenced. The deduced gene products exhibited the highest similarity to the corresponding subunits of the cyanobacterial bidirectional soluble hydrogenases (HoxEFUYH). The five genes were localized on a single transcript according to reverse transcription-PCR experiments. A 54 -type promoter preceded the gene cluster, suggesting that there was inducible expression of the operon. The Hox hydrogenase was proven to function as a truly bidirectional hydrogenase; it produced H 2 under nitrogenase-repressed conditions, and it recycled the hydrogen produced by the nitrogenase in cells fixing N 2 . In-frame deletion of the hoxE gene eliminated hydrogen evolution derived from the Hox enzyme in vivo, although it had no effect on the hydrogenase activity in vitro. This suggests that HoxE has a hydrogenase-related role; it likely participates in the electron transfer processes. This is the first example of the presence of a cyanobacterial-type, NAD ؉ -reducing hydrogenase in a phototrophic bacterium that is not a cyanobacterium. The potential physiological implications are discussed.

show abstract

Section: Resultsmentioning

confidence: 99%

Cyanobacterial-Type, Heteropentameric, NAD ⁺ -Reducing NiFe Hydrogenase in the Purple Sulfur Photosynthetic Bacterium Thiocapsa roseopersicina

Rákhely

Kovács

Maróti

et al. 2004

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…The expression of hydrogenase genes in Synechococcus sp. PCC 7942 is under the control of the circadian clock, as shown for two promoters of the gene cluster (186). When expressed, the native protein might function as a dimeric assembly complex Hox(EFUYH) 2 (188).…”

Section: Hydrogenases In Cyanobacteria Hydrogenase Types In Cyanobactmentioning

confidence: 99%

“…In Synechococcus sp. PCC 7942 (ϭ Anacystis nidulans), the genes are organized into two clusters, hoxEF and hoxUYHWhypAB, and are regulated by three promoters, one before each of hoxE, hoxU, and hoxW (23,186). In Synechocystis sp.…”

Section: Hydrogenases In Cyanobacteria Hydrogenase Types In Cyanobactmentioning

confidence: 99%

Nitrogen Fixation and Hydrogen Metabolism in Cyanobacteria

Bothe

Schmitz²,

Yates

et al. 2010

Microbiol Mol Biol Rev

Self Cite

344

219

View full text Add to dashboard Cite

SUMMARY This review summarizes recent aspects of (di)nitrogen fixation and (di)hydrogen metabolism, with emphasis on cyanobacteria. These organisms possess several types of the enzyme complexes catalyzing N2 fixation and/or H2 formation or oxidation, namely, two Mo nitrogenases, a V nitrogenase, and two hydrogenases. The two cyanobacterial Ni hydrogenases are differentiated as either uptake or bidirectional hydrogenases. The different forms of both the nitrogenases and hydrogenases are encoded by different sets of genes, and their organization on the chromosome can vary from one cyanobacterium to another. Factors regulating the expression of these genes are emerging from recent studies. New ideas on the potential physiological and ecological roles of nitrogenases and hydrogenases are presented. There is a renewed interest in exploiting cyanobacteria in solar energy conversion programs to generate H2 as a source of combustible energy. To enhance the rates of H2 production, the emphasis perhaps needs not to be on more efficient hydrogenases and nitrogenases or on the transfer of foreign enzymes into cyanobacteria. A likely better strategy is to exploit the use of radiant solar energy by the photosynthetic electron transport system to enhance the rates of H2 formation and so improve the chances of utilizing cyanobacteria as a source for the generation of clean energy.

show abstract

“…In Synechococcus sp. strain PCC 7942, hoxEF and hoxUYHW are located on two different transcripts (40). hoxUYHW may be polycistronic, with a second promoter located between hoxH and hoxW (40).…”

mentioning

confidence: 99%

“…strain PCC 7942, hoxEF and hoxUYHW are located on two different transcripts (40). hoxUYHW may be polycistronic, with a second promoter located between hoxH and hoxW (40). The differences in structural gene organization and transcription units may imply a difference in transcriptional regulation between different strains.…”

mentioning

confidence: 99%

Transcription and Regulation of the Bidirectional Hydrogenase in the Cyanobacterium Nostoc sp. Strain PCC 7120

Sjöholm

Oliveira

Lindblad

2007

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

Quantitative analysis of expression of two circadian clock‐controlled gene clusters coding for the bidirectional hydrogenase in the cyanobacterium Synechococcus sp. PCC7942

Cited by 30 publications

References 30 publications

Cyanobacterial-Type, Heteropentameric, NAD ⁺ -Reducing NiFe Hydrogenase in the Purple Sulfur Photosynthetic Bacterium Thiocapsa roseopersicina

Cyanobacterial-Type, Heteropentameric, NAD ⁺ -Reducing NiFe Hydrogenase in the Purple Sulfur Photosynthetic Bacterium Thiocapsa roseopersicina

Nitrogen Fixation and Hydrogen Metabolism in Cyanobacteria

Transcription and Regulation of the Bidirectional Hydrogenase in the Cyanobacterium Nostoc sp. Strain PCC 7120

Contact Info

Product

Resources

About

Quantitative analysis of expression of two circadian clock‐controlled gene clusters coding for the bidirectional hydrogenase in the cyanobacterium Synechococcus sp. PCC7942

Cited by 30 publications

References 30 publications

Cyanobacterial-Type, Heteropentameric, NAD + -Reducing NiFe Hydrogenase in the Purple Sulfur Photosynthetic Bacterium Thiocapsa roseopersicina

Cyanobacterial-Type, Heteropentameric, NAD + -Reducing NiFe Hydrogenase in the Purple Sulfur Photosynthetic Bacterium Thiocapsa roseopersicina

Nitrogen Fixation and Hydrogen Metabolism in Cyanobacteria

Transcription and Regulation of the Bidirectional Hydrogenase in the Cyanobacterium Nostoc sp. Strain PCC 7120

Contact Info

Product

Resources

About

Cyanobacterial-Type, Heteropentameric, NAD ⁺ -Reducing NiFe Hydrogenase in the Purple Sulfur Photosynthetic Bacterium Thiocapsa roseopersicina

Cyanobacterial-Type, Heteropentameric, NAD ⁺ -Reducing NiFe Hydrogenase in the Purple Sulfur Photosynthetic Bacterium Thiocapsa roseopersicina