The nifEN genes participating in FeMo cofactor biosynthesis and genes encoding dinitrogenase are part of the same operon in Bradyrhizobium species

Om, Aguilar; Taormino, J P; Thöny, Beat; Ramseier, Tom M.; Hennecke, Hauke; Aa, Szalay

doi:10.1007/bf00262436

Cited by 20 publications

(16 citation statements)

References 42 publications

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“…NGR234 (46% identity, 61% similarity) [16]. The second contiguous ORF had homology with the nifN gene product from B. japonicum (46% identity, 61% similarity) [15] and Rhizobium sp. (41% identity, 57% similarity) [16].…”

Section: Identi¢cation Of Nifenxorf1orf2 Genes Of H Seropedicaementioning

confidence: 99%

“…A BLAST search of the GenBank database showed that the ¢rst one had high identity with the nifE gene product from Bradyrhizobium japonicum (52% identity, 65% similarity) [15] and Rhizobium sp. NGR234 (46% identity, 61% similarity) [16].…”

Section: Identi¢cation Of Nifenxorf1orf2 Genes Of H Seropedicaementioning

confidence: 99%

“…(41% identity, 57% similarity) [16]. The NifD-NifE, NifK-NifN protein pairs from H. seropedicae showed conserved amino [15] and Rhizobium sp. [16].…”

Section: Identi¢cation Of Nifenxorf1orf2 Genes Of H Seropedicaementioning

confidence: 99%

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Sequencing and functional analysis of the nifENXorf1orf2 gene cluster of Herbaspirillum seropedicae

Klassen¹

1999

FEMS Microbiology Letters

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A 5.1-kb DNA fragment from the nifHDK region of H. seropedicae was isolated and sequenced. Sequence analysis showed the presence of nifENXorf1orf2 but nifTY were not present. No nif or consensus promoter was identified. Furthermore, orf1 expression occurred only under nitrogen-fixing conditions and no promoter activity was detected between nifK and nifE, suggesting that these genes are expressed from the upstream nifH promoter and are parts of a unique nif operon. Mutagenesis studies indicate that nifN was essential for nitrogenase activity whereas nifXorf1orf2 were not. High homology between the C-terminal region of the NifX and NifB proteins from H. seropedicae was observed. Since the NifX and NifY proteins are important for FeMo cofactor (FeMoco) synthesis, we propose that alternative proteins with similar activities exist in H. seropedicae. ß

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Section: Identi¢cation Of Nifenxorf1orf2 Genes Of H Seropedicaementioning

confidence: 99%

Section: Identi¢cation Of Nifenxorf1orf2 Genes Of H Seropedicaementioning

confidence: 99%

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Sequencing and functional analysis of the nifENXorf1orf2 gene cluster of Herbaspirillum seropedicae

Klassen¹

1999

FEMS Microbiology Letters

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“…Indeed, phylogenetic analysis suggests that DPOR may be more closely related to another NifDK-like protein pair known as NifE and NifN. 2 The NifEN complex, which is thought to play a possible redox role in the FeMo cofactor biosynthesis (37), also has a similar partial conservation of the P cluster Cys residues (three in NifE and only one in NifN) (38,39). Studies have shown that NifEN contains two 4Fe-4S clusters instead of the two 8Fe:7S P clusters that are present in NifDK (37).…”

Section: Discussionmentioning

confidence: 99%

Reconstitution of Light-independent Protochlorophyllide Reductase from Purified Bchl and BchN-BchB Subunits

Fujita¹,

Bauer

2000

Journal of Biological Chemistry

165

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Protochlorophyllide reductase catalyzes the reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls and bacteriochlorophylls. The light-independent (dark) form of protochlorophyllide reductase plays a key role in the ability of gymnosperms, algae, and photosynthetic bacteria to green (form chlorophyll) in the dark. Genetic and sequence analyses have indicated that dark protochlorophyllide reductase consists of three protein subunits that exhibit significant sequence similarity to the three subunits of nitrogenase, which catalyzes the reductive formation of ammonia from dinitrogen. However, unlike the well characterized features of nitrogenase, there has been no previous biochemical characterization of dark protochlorophyllide reductase. In this study, we report the first reproducible demonstration of dark protochlorophyllide reductase activity from purified protein subunits that were isolated from the purple nonsulfur photosynthetic bacterium Rhodobacter capsulatus. Two of the three subunits (Bchl and BchN) were expressed in R. capsulatus as S tag fusion proteins that facilitated affinity purification. The third subunit (BchB) was co-purified with the BchN protein indicating that BchN and BchB proteins form a tight complex. Dark protochlorophyllide reductase activity was shown to be dependent on the presence of all three subunits, ATP, and the reductant dithionite. The similarity of dark protochlorophyllide reductase to nitrogenase is discussed.

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“…Comparison of the predicted amino acid sequences of the Azospirillum brasilense (ab) NifE (I), NifN (II), NifX (III) and NifQ (IV) proteins with analogous gene products from Azotobacter vinelandii (av) (4), Klebsiella pneumoniae (kp) (37,38), Gluconacetobacter diazotrophicus (ad) (9), Rhodobacter capsulatus (rc) (16), Bradyrhizobium japonicum (bj) (31), Herbaspirillum seropedicae (hs) (10), Rhizobium sp (rsp) (36), and Enterobacter agglomerans (ea) (35). A black background indicates conserved residues in all aligned sequences, dark grey indicates conserved residues in at least 80% of the aligned sequences, and light grey indicates conserved residues in at least 60% of the aligned sequences.…”

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confidence: 99%

Sequencing and promoter analysis of the nifENXorf3orf5fdxAnifQ operon from Azospirillum brasilense Sp7

Potrich

Bressel

Schrank

et al. 2001

Braz J Med Biol Res

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A 40-kb DNA region containing the major cluster of nif genes has been isolated from the Azospirillum brasilense Sp7 genome. In this region three nif operons have been identified: nifHDKorf1Y, nifENXorf3orf5fdxAnifQ and orf2nifUSVorf4. The operons containing nifENX and nifUSV genes are separated from the structural nifHDKorf1Y operon by about 5 kb and 10 kb, respectively. The present study shows the sequence analysis of the 6045-bp DNA region containing the nifENX genes. The deduced amino acid sequences from the open reading frames were compared to the nif gene products of other diazotrophic bacteria and indicate the presence of seven ORFs, all reading in the same direction as that of the nifHDKorf1Y operon. Consensus I 54 and NifA-binding sites are present only in the promoter region upstream of the nifE gene. This promoter is activated by NifA protein and is approximately two-times less active than the nifH promoter, as indicated by the ß-galactosidase assays. This result suggests the differential expression of the nif genes and their respective products in Azospirillum.

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The nifEN genes participating in FeMo cofactor biosynthesis and genes encoding dinitrogenase are part of the same operon in Bradyrhizobium species

Cited by 20 publications

References 42 publications

Sequencing and functional analysis of the nifENXorf1orf2 gene cluster of Herbaspirillum seropedicae

Sequencing and functional analysis of the nifENXorf1orf2 gene cluster of Herbaspirillum seropedicae

Reconstitution of Light-independent Protochlorophyllide Reductase from Purified Bchl and BchN-BchB Subunits

Sequencing and promoter analysis of the nifENXorf3orf5fdxAnifQ operon from Azospirillum brasilense Sp7

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