Multiple copies of genes coding for electron transport proteins in the bacterium Nitrosomonas europaea

McTavish, Hugh; LaQuier, F W; Arciero, David M.; Logan, M; Mundfrom, Gary; Fuchs, James A.; Hooper, Alan B.

doi:10.1128/jb.175.8.2445-2447.1993

Cited by 54 publications

(56 citation statements)

References 26 publications

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“…The sequences for these peptides were 1,200 bp from the 3' end of hao. These results agree with previous observations and the suggestion that the gene for Cyt c-554 was located approximately 2,700 bp from hao (15). The XHAO-1 clone unfortunately contained only part of the ORF for Cyt c-554.…”

Section: Resultssupporting

confidence: 83%

“…lc), was used in Southern hybridizations to estimate the copy number of hao. Genomic DNA digested with BamHI, EcoRI, KpnI, Sall, SmaI, and XhoI (data not shown) showed hybridization patterns similar to those previously reported (11,15). These hybridizations confirmed the presence of three copies of hao in N. europaea and eliminated the ambiguity resulting from the use of degenerate oligonucleotides.…”

Section: Resultssupporting

confidence: 68%

“…While knowledge of the biochemistry of HAO has continued to increase, the genetic information has remained limited. The genome of N. europaea apparently contains three copies of the genes for HAO and Cyt c-554 (15).…”

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confidence: 99%

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Characterization of the gene encoding hydroxylamine oxidoreductase in Nitrosomonas europaea

1994

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Hydroxylamine oxidoreductase (HAO) catalyzes the oxidation of hydroxylamine to nitrite in Nitrosomonas europaea. The electrons released in the reaction are partitioned to ammonium monooxygenase and to the respiratory chain. The immediate acceptor of electrons from HAO is believed to be cytochrome c-554 (Cyt c-554). We have isolated a genomic DNA fragment containing the structural gene encoding HAO (hao) and a part of the gene for Cyt c-554. The nucleotide sequence of hao was determined, and its transcription was analyzed. The open reading frame (ORF) encodes amino acid sequences matching the purified peptides of HAO. A 64.28-kDa protein is encoded in this ORF, in close agreement with the empirically determined molecular mass of 63 kDa. The N terminus was located 24 amino acids from the start codon, suggesting the presence of a leader sequence. The putative eight heme-binding peptides were localized in this ORF. The gene for Cyt c-554 was located 1,200 bp downstream from the 3' end of hao. An ORF was identified in the upstream region from hao and may encode a protein of unknown function. Data bank searches did not reveal proteins with substantial similarities to HAO, but they did reveal similarities between Cyt c-554 and other c-type cytochromes.

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Section: Resultssupporting

confidence: 83%

Section: Resultssupporting

confidence: 68%

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Characterization of the gene encoding hydroxylamine oxidoreductase in Nitrosomonas europaea

1994

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“…europaea has been characterized and is closely linked to the hcy gene encoding cytochrome csS4, which may be the primary electron acceptor for H A 0 Sayavedra-Soto et al, 1994;Arciero et al, 1991). Three copies each of the hao and hcy genes are present in the N. europaea genome (McTavish et al, 1993a).…”

Section: Chemolithoautotrophic Nitrifying Bacteria Such Asmentioning

confidence: 99%

“…Genes designated p m o A and pmoB have been characterized, and the nucleotide sequence of a third gene, pmoC, is described in the sequence databases (Semrau et al, 1995;Zahn & DiSpirito, 1996; accession numbers L40804 and U94337). The A M 0 is also believed to be encoded by three genes, amoA, amoB and amoC, of which there are two copies each in the N. europaea genome (McTavish et al, 1993a, b ;Klotz et al, 1997).…”

Section: Chemolithoautotrophic Nitrifying Bacteria Such Asmentioning

confidence: 99%

Heterologous expression of heterotrophic nitrification genes

Crossman

Moir²,

Enticknap³

et al. 1997

Microbiology

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Paracoccus denitrificans is a heterotrophic organism capable of oxidizing ammonia to nitrite during growth on an organic carbon and energy source. This pathway, termed heterotrophic nitrification, requires the concerted action of an ammonia monooxygenase (AMO) and hydroxylamine oxidase (HAO). The genes required for heterotrophic nitrification have been isolated by introducing a Pa. denitrificans genomic library into Pseudomonas putida and screening for the accumulation of nitrite. In contrast to the situation in chemolithoautotrophic ammonia oxidizers, the genes encoding AM0 and HA0 are present in single linked copies in the genome of Pa. denitrificans-AM0 from Pa. denitrificans expressed in Ps. putida is capable of oxidizing ethene (ethylene) to epoxyethane (ethylene oxide), which is indicative of a relaxed substrate specificity. Further, when expressed in the methylotroph Methylobacterium extorquens AMI, the AM0 endows on this organism the ability to grow on ethene and methane. Thus, the Pa. denitrificans AM0 is capable of oxidizing methane t o methanol, as is the case for the AM0 from Nitrosomonas europaea. The heterotrophic nitrification genes are moderately toxic in M. extorquens, more toxic in Ps. putida, and non-toxic in Escherichia coli. Toxicity is due t o the activity of the gene products in M. extorquens, and both expression and activity in Ps. putida. This is the first time that the genes encoding an active AM0 have been expressed in a heterologous host.

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Nitrifikation - Grundlagen des Stoffwechsels und Probleme bei der Nutzung von Ammoniakoxidanten

Schmidt¹,

Gries²,

Willuweit³

1999

Acta hydrochim. hydrobiol.

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Multiple copies of genes coding for electron transport proteins in the bacterium Nitrosomonas europaea

Cited by 54 publications

References 26 publications

Characterization of the gene encoding hydroxylamine oxidoreductase in Nitrosomonas europaea

Characterization of the gene encoding hydroxylamine oxidoreductase in Nitrosomonas europaea

Heterologous expression of heterotrophic nitrification genes

Nitrifikation - Grundlagen des Stoffwechsels und Probleme bei der Nutzung von Ammoniakoxidanten

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