Carboxy‐terminal processing of the large subunit of [NiFe] hydrogenases

Menon, N; Robbins, Jeff; Vartanian, Marie Der; Patil, Daulat S.; Peck, Harry D.; Menon, Angeli Lal; Robson, Richard M.; Przybyla, Alan

doi:10.1016/0014-5793(93)80303-c

Cited by 56 publications

(30 citation statements)

References 22 publications

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“…It remains to be shown how the HoxYH proteins are integrated into or transferred across the cytoplasmic membrane. The amino acids processed from the carboxy-terminus of the immature HoxH possibly play a role in this insertion, as suggested for the D. gigas hydrogenase [28]. For comparison, the NAD+-reducing hydrogenase from A. eutrophus resides in the cytoplasm [49], but the coenzyme-F4,0-reducing enzymes from M. voltae [50, 511 and from Methanosurcina barkeri [52], though lacking signal peptides [SO], appear to be at least partly associated with the cytoplasmic membrane as shown by immunogold labeling.…”

Section: Discussionmentioning

confidence: 86%

Molecular Biological Analysis of a Bidirectional Hydrogenase from Cyanobacteria

Schmitz

Boison

Hilscher

et al. 1995

European Journal of Biochemistry

147

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: Discussionmentioning

confidence: 86%

Molecular Biological Analysis of a Bidirectional Hydrogenase from Cyanobacteria

Schmitz

Boison

Hilscher

et al. 1995

European Journal of Biochemistry

147

162

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“…The biosynthesis of NiFe hydrogenases is closely related to Ni metabolism, both to form an active enzyme and at the transcriptional level (101,135,211,212). Cyanobacterial hydrogenases seem to be no exception.…”

Section: Cyanobacterial Uptake Hydrogenasesmentioning

confidence: 99%

“…The maturation of nickel-containing enzymes, e.g., hydrogenases, ureases, and carbon monoxide dehydrogenases, is a complex process requiring accessory proteins (42,81,122,127,135,211,213). Initial work using E. coli revealed five ORFs, designated hypABCDE, affecting hydrogenases pleiotropically (119).…”

Section: Accessory Genesmentioning

confidence: 99%

Hydrogenases and Hydrogen Metabolism of Cyanobacteria

Tamagnini

Axelsson

Lindberg

et al. 2002

Microbiol Mol Biol Rev

466

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 maturation of hydrogenases is a complex process requiring a number of accessory proteins (Menon et al, 1993;Vignais & Toussaint, 1994;Maier & Triplett, 1996;Buhrke et al, 2001;Casalot & Rousset, 2001;Vignais et al, 2001;Blokesch et al, 2002;Paschos et al, 2002). One distinct feature in the NiFe-hydrogenases maturation process is the endoproteolytic cleavage of a C-terminal peptide of the large subunit precursor, carried out by a specific C-terminal endopeptidase (Casalot & Rousset, 2001;Paschos et al, 2002).…”

Section: Introductionmentioning

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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Carboxy‐terminal processing of the large subunit of [NiFe] hydrogenases

Cited by 56 publications

References 22 publications

Molecular Biological Analysis of a Bidirectional Hydrogenase from Cyanobacteria

Molecular Biological Analysis of a Bidirectional Hydrogenase from Cyanobacteria

Hydrogenases and Hydrogen Metabolism of Cyanobacteria

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

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