The biosynthesis of periplasmic electron transport proteins in methylotrophic bacteria

Goodwin, P. M.; Anthony, Christopher

doi:10.1099/13500872-141-5-1051

Cited by 30 publications

(20 citation statements)

References 96 publications

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“…In Gram‐negative methylotrophic bacteria, methanol is oxidised by methanol dehydrogenase (MDH), a quinoprotein with an α 2 β 2 tetrameric structure, containing pyrrolo‐quinoline quinone (PQQ) and a calcium ion at its active site. Its electron acceptor is a specific c ‐type cytochrome, usually designated cytochrome c L [1, 2]. There are at least 30 methanol oxidation genes, arranged in 5 clusters; these include the genes involved in PQQ biosynthesis [2].…”

Section: Introductionmentioning

confidence: 99%

“…Its electron acceptor is a specific c ‐type cytochrome, usually designated cytochrome c L [1, 2]. There are at least 30 methanol oxidation genes, arranged in 5 clusters; these include the genes involved in PQQ biosynthesis [2]. The genes encoding the α and β subunits of MDH ( mxaF and I ) and cytochrome c L ( mxaG ) are situated in an operon together with mxaJ [3–5].…”

Section: Introductionmentioning

confidence: 99%

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The methanol oxidation genes mxaFJGIR(S)ACKLD in Methylobacterium extorquens

Amaratunga

Goodwin

O’Connor

et al. 2006

FEMS Microbiology Letters

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MxaJ is a protein of unknown function encoded by mxaJ in the mxaFJGI operon. We have constructed a mxaJ mutant of M. extorquens with a deletion which does not affect transcription of downstream genes. It contained cytochrome cL (MxaG), but neither subunit of methanol dehydrogenase (MxaF and MxaI). MxaJ is probably involved in processing this enzyme. We have sequenced the region between mxaFJGI and five other methanol oxidation genes, mxaACKLD; it includes one open reading frame (mxaR) and a possible second open reading frame (mxaS), demonstrating the presence in M. extorquens of the following gene cluster: mxaFJGIR(S) ACKLD.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The methanol oxidation genes mxaFJGIR(S)ACKLD in Methylobacterium extorquens

Amaratunga

Goodwin

O’Connor

et al. 2006

FEMS Microbiology Letters

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“…Since an NAD+-dependent methanol dehydrogenase is also known (Arfman et al, 1989), it is suggested to use the abbreviation QMDH for the PQQ-dependent dehydrogenase and MDH for the NAD+-dependent methanol dehydrogenase. The QMDH is connected to an electron transport chain that, in contrast to P. aerzkginosa, consists of the two soluble cytochromes cL and c H , and a cytochrome oxidase (Goodwin & Anthony, 1995). In M. extorquens, cytochrome cL is the direct electron acceptor of QMDH; it shows little similarity to other known cytochromes (Nunn & Anthony, 1988).…”

Section: Af068264mentioning

confidence: 99%

Cytochrome C550 is an essential component of the quinoprotein ethanol oxidation system in Pseudomonas aeruginosa: cloning and sequencing of the genes encoding cytochrome C550 and an adjacent acetaldehyde dehydrogenase

Schobert¹,

Görisch²

1999

Microbiology

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Pseudomonas aeruginosa ATCC 17933 grown aerobically on ethanol produces a soluble cytochrome c5, together with a quinoprotein ethanol dehydrogenase. A 3 2 kb genomic DNA fragment containing the gene encoding cytochrome c550 was cloned and sequenced. Two other complete and two truncated ORFs were also identified. A truncated ORF encoding the quinoprotein ethanol dehydrogenase (exaA) was found upstream of the cytochrome c550 gene (exaB) and in reverse orientation. An ORF encoding a NAD+-dependent acetaldehyde dehydrogenase (exaC) was located downstream of the cytochrome c, , , gene and in the same orientation. Another ORF showed similarity to the pqqA gene and a truncated ORF similarity t o the pgqB gene, both involved in the biosynthesis of the prosthetic group PQQ. The organization of these genes was found to be different from the well-studied methanol oxidation system in methylotrophic bacteria. The deduced amino acid sequence of cytochrome c550 from P. aenrginosa showed some similarity t o cytochrome c, of the alga Chlamydomonas reinhanltii and the haem domain of quinohaemoprotein alcohol dehydrogenases of acetic acid bacteria, but no similarity t o the soluble cytochrome c, o f the quinoprotein methanol oxidation system of methylotrophs could be detected. A mutant of P. aeruginosa with an interrupted cytochrome c550 gene was unable to grow on ethanol, which proves that cytochrome csso is an essential component of the ethanol oxidation system in this organism.

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“…The fairly close correlation between the expression of the putative methanol porin and methanol dehydrogenase during the growth of M. methylotrophus under various conditions suggests that expression of these proteins may be regulated in concert. The mechanism via which methanol oxidation is regulated in methylotrophic bacteria remains to be determined, but probably occurs via a complex and hierarchical process involving at least two sensor‐regulator systems, one of which responds to the presence of methanol and/or formaldehyde (see [1, 12]).…”

Section: Discussionmentioning

confidence: 99%

“…The methylotrophic bacterium Methylophilus methylotrophus grows readily on methanol as a source of carbon. The methanol is initially oxidised by a periplasmic, pyrroloquinoline quinone‐ (PQQ‐) and Ca 2+ ‐containing methanol dehydrogenase (see[1]), and the resultant formaldehyde passes into the cytoplasm before being further metabolised via the ribulose monophosphate pathway[2]. Although bacteria contain a wide variety of outer‐membrane porins [3, 4], it has generally been assumed that small, uncharged molecules such as methanol, traverse bacterial membranes by simple diffusion.…”

Section: Introductionmentioning

confidence: 99%

Purification, properties and physiological regulation of a putative outer-membrane porin for methanol in Methylophilus methylotrophus

Greenwood

Mills

Jones

2006

FEMS Microbiology Letters

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A major outer‐membrane protein was purified and partially characterised from the methylotrophic bacterium Methylophilus methylotrophus. The protein had a subunit Mr of 38 000 and was similar in terms of its biochemical properties to the recently characterised amide‐urea porin (FmdC) from the same organism. Expression of the protein, as determined by SDS‐PAGE and Western blotting of cells grown in continuous culture under various nutrient limitations, varied in a similar manner to that of methanol dehydrogenase and was maximal under methanol limitation. It was concluded that the protein is probably an outer‐membrane porin for methanol.

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The biosynthesis of periplasmic electron transport proteins in methylotrophic bacteria

Cited by 30 publications

References 96 publications

The methanol oxidation genes mxaFJGIR(S)ACKLD in Methylobacterium extorquens

The methanol oxidation genes mxaFJGIR(S)ACKLD in Methylobacterium extorquens

Cytochrome C550 is an essential component of the quinoprotein ethanol oxidation system in Pseudomonas aeruginosa: cloning and sequencing of the genes encoding cytochrome C550 and an adjacent acetaldehyde dehydrogenase

Purification, properties and physiological regulation of a putative outer-membrane porin for methanol in Methylophilus methylotrophus

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