Some properties of the nickel-containing hydrogenase of chemolithotrophically grown Rhizobium japonicum

Harker, Alan R.; Xu, Lang-Lai; Hanus, F. J.; Evans, Harold J.

doi:10.1128/jb.159.3.850-856.1984

Cited by 62 publications

(19 citation statements)

References 43 publications

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“…In the same experiment, the Oa-dependent hydrogenase activities of bacteroids from the wild-type UPM791 and AL91 strains were 1200 and 870 nmol of Hg oxidized per hour and mg protein, respectively. Since methyiene blue is a primary electron acceptor from the hydrogenase (Harker et al, 1984). these results indicate that the hyp cluster is essential for hydrogenase synthesis in R. leguminosarum bv.…”

Section: Characterization Of T/75 Hup~ Mutantsmentioning

confidence: 68%

Molecular analysis of a microaerobically induced operon required for hydrogenase synthesis in Rhizobium leguminosarum biovar viciae

Rey

Murillo

Hernando

et al. 1993

Molecular Microbiology

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The nucleotide sequence (6138 bp) of a microaerobically inducible region (hupV/VI) from the Rhizobium leguminosarum bv. viciae hydrogenase gene cluster has been determined. Six genes, arranged as a single operon, were identified, and designated hypA, B, F, C, D and E based on the sequence similarities of all of them, except hypF, to genes from the hydrogenase pleiotropic operon (hyp) from Escherichia coli. The gene products from hypBFCDE were identified by in vivo expression analysis in E. coli, and their molecular sizes were consistent with those predicted from the nucleotide sequence. Transposon Tn5 insertions into hypB, hypF, hypD and hypE resulted in R. leguminosarum mutants that lacked any hydrogenase activity in symbiosis with peas, but still were able to synthesize the polypeptide for the hydrogenase large subunit. The gene products HypA, HypB, HypF and HypD contained CX2C motifs characteristic of metal-binding proteins. In addition, HypB bore a long histidine-rich stretch of amino acids near the N-terminus, suggesting a possible role in nickel binding for this protein. The gene product HypF, which was translationally coupled to HypB, presented two cysteine motifs (CX2CX18CX2C) with a capacity to form zinc finger-like structures in the N-terminal third of the protein. A role in nickel metabolism in relation to hydrogenase synthesis is postulated for proteins HypB and HypF.

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Section: Characterization Of T/75 Hup~ Mutantsmentioning

confidence: 68%

Molecular analysis of a microaerobically induced operon required for hydrogenase synthesis in Rhizobium leguminosarum biovar viciae

Rey

Murillo

Hernando

et al. 1993

Molecular Microbiology

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“…They include Rhodobacter capsulatus [16,45], Rhodocyclus gelatinosus [17], Bradyrhizobium japonicum [18,46], Rhizobium leguminosarum [19,20,47], Azotobacter chroococcum [21], Azotobacter vinelandii [22,48], Wolinella succinogenes [24] and Escherichia coli (isoenzymes 1 and 2, Table 1) ( [23,49,50]; Menon, N.K., Robbins, J., DerVartanian, D.V., Choi, E.C. and Przybyla, A.E., personal communication).…”

Section: He-uptake Membrane-bound Nife-hydrogenasesmentioning

confidence: 99%

Microbial hydrogenases: Primary structure, classification, signatures and phylogeny

Mandrand

1993

FEMS Microbiology Letters

191

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Thirty sequenced microbial hydrogenases are classified into six classes according to sequence homologies, metal content and physiological function. The first class contains nine H2‐uptake membrane‐bound NiFe‐hydrogenases from eight aerobic, facultative anaerobic and anaerobic bacteria. The second comprises four periplasmic and two membrane‐bound H2 ‐uptake NiFe(Se)‐hydrogenases from sulphate‐reducing bacteria. The third consists of four periplasmic Fe‐hydrogenases from strict anaerobic bacteria. The fourth contains eight methyl‐viologen‐ (MV), factor F420‐ (F420) or NAD‐reducing soluble hydrogenases from methanobacteria and Alcaligenes eutrophus H16. The fifth is the H2‐producing labile hydrogenase isoenzyme 3 of Escherichia coli. The sixth class contains two soluble tritium‐exchange hydrogenases of cyanobacteria. The results of sequence comparison reveal that the 30 hydrogenases have evolved from at least three different ancestors. While those of class I, II, IV and V hydrogenases are homologous, i.e. sharing the same evolutionary origin, both class III and VI hydrogenases are neither related to each other nor to the other classes. Sequence comparison scores, hierarchical cluster structures and phylogenetic trees show that class II falls into two distinct clusters composed of NiFe‐ and NiFeSe‐hydrogenases, respectively. These results also reveal that class IV comprises three distinct clusters: MV‐reducing, F420‐reducing and NAD‐reducing hydrogenases. Specific signatures of the six classes of hydrogenases as well as some subclusters have been detected. Analyses of motif compositions indicate that all hydrogenases, except those of class VI, must contain some common motifs probably participating in the formation of hydrogen activation domains and electron transfer domains. The regions of hydrogen activation domains are highly conserved and can be divided into two categories. One corresponds to the ‘nickel active center’ of NiFe(Se)‐hydrogenases. It consists of two possible specific nickel‐binding motifs, RxCGxCxxxH and DPCxxCxxH, located at the N‐ and C‐termini of so‐called large subunits in the dimeric hydrogenases, respectively. The other is the H‐cluster of the Fe‐hydrogenases. It might comprise three motifs on the C‐terminal half of the large subunits. However, the motifs corresponding to the putative electron transfer domains, as well as their polypeptides chains, are poorly or even not at all conserved. They are present essentially on the small subunits in NiFe‐hydrogenases. Some of these motifs resemble the typical ferredoxin‐like Fe‐S cluster binding site. The variation of the sequences in these regions might determine the specific interaction between the external electron transfer domains of hydrogenases and their electron carriers. For example, the C‐terminal cysteine‐histidine rich region of the small subunits are distinguishable between those of H2‐uptake, H2‐producing, MV‐reducing, F420‐reducing and NAD‐reducing NiFe(Se)‐hydrogenases.

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“…This nickel-containing hydrogenase (Arp. 1985;Harker et at., 1984;Stults ef ai, 1984) is composed of 33 and 65 kDa subunits encoded by hupS and hupL, respectively (Sayavedra-Soto etat., 1988), Using plasmid-borne tiup-iacZ fusions, it was found that nickel, hydrogen, and oxygen transcriptionaliy r'egulate expression of the operon through a common c/s-acting region 5' of the promoter (Kim and Maier, 1990;Kim etai. 1991).…”

Section: Introductionmentioning

confidence: 99%

IHF‐ and RpoN‐dependent regulation c hydrogenase expression in Bradyrhizobium japonicum

Black

Maier

1995

Molecular Microbiology

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Sequence analysis of the Bradyrhizobium japonicum hydrogenase promoter regulatory region indicated the presence of a -24/-12 type promoter, which is recognized by RpoN, and a potential integration host factor (IHF)-binding site. B. japonicum rpoN1-/rpoN2- double mutants were deficient in hydrogen-uptake activity. Using plasmid-borne hup-lacZ fusions, it was shown that the rpoN mutants were also deficient in nickel-dependent transcriptional regulation of hydrogenase. Gel-shift assays of the hydrogenase promoter regulatory region showed that purified IHF from Escherichia coli binds to a 210 bp fragment. DNase footprint analysis revealed a protected region of 31 bp between bases -44 and -75 from the transcription start site. Western analysis with B. japonicum soluble extract and antibodies against E. coli IHF gave two bands equivalent to molecular masses of 12 and 14 kDa approximately. When the IHF-binding area is mutated on a plasmid-borne hup-lacZ fusion, nickel-dependent transcriptional regulation of hydrogenase is still observed, but the transcriptional rates are clearly less than in the parent hup-lacZ fusion plasmid. Like the results with nickel, regulation of hydrogenase by other transcriptional regulators (hydrogen and oxygen) still occurs, but at a diminished level in the IHF-binding-area-mutated construct.

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Some properties of the nickel-containing hydrogenase of chemolithotrophically grown Rhizobium japonicum

Cited by 62 publications

References 43 publications

Molecular analysis of a microaerobically induced operon required for hydrogenase synthesis in Rhizobium leguminosarum biovar viciae

Molecular analysis of a microaerobically induced operon required for hydrogenase synthesis in Rhizobium leguminosarum biovar viciae

Microbial hydrogenases: Primary structure, classification, signatures and phylogeny

IHF‐ and RpoN‐dependent regulation c hydrogenase expression in Bradyrhizobium japonicum

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