The Energy Conserving N5‐Methyltetrahydromethanopterin:Coenzyme M Methyltransferase Complex from Methanobacterium thermoautotrophicum is Composed of Eight Different Subunits

Harms, Ulrike; Weiss, David S.; Gärtner, Peter; Linder, Dietmar; Thauer, Rudolf K.

doi:10.1111/j.1432-1033.1995.0640m.x

Cited by 71 publications

(60 citation statements)

References 40 publications

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“…A., FitzGerald, L. M., Clayton, R. A., Gocaine, J. and H 2 , the H 2 being subsequently used in the reduction of the D., Kerlavage, A. R., Dougherty, B. A., Tomb, J. F., Adams, M. D., methyl group of acetyl-CoA to methane (Kemner et al, 1987; Reich, C. I., Overbeek, R., Kirkness, E. F., Weinstock, K. G., Merrik, Kemner and Zeikus, 1994;Lovely and Ferry, 1985; Fischer and J. M., Glodek, A., Scott, J. L., Geoghagen, N. S. M., Weidman, J. F., Fuhrmann, J. L., Nguyen, D., Utterback, T. R., Kelley, J. M., Thauer, 1990; for a recent review see Ferry, 1997) The latter Peterson, J. D., Sadow, P. W., Hanna, M. C., Cotton, M. D., Roberts, reaction has also been shown to be coupled with energy conser-K. M., Hurst, M. A., Kaine, P. P., Borodovsky, M., Klenk, H. P., vation (Deppenmeier et al, 1996).…”

Section: Polypeptidementioning

confidence: 99%

“…for most proteins of the N 5 -methyl-tain, as HycE, a carboxy-terminal peptide immediately adjacent tetrahydromethanopterin:coenzyme M methyltransferase com-to the last amino acid of the conserved nickel-binding motif. plex from M. thermoautotrophicum (Harms et al, 1995).…”

Section: Polypeptidementioning

confidence: 99%

“…Protein was concentrated these motifs, it shows almost no sequence similarity to other by ultrafiltration using Molecular/pore membranes (cut-off [NiFe] hydrogenases with one exception; it is similar (37 % 50 kDa; Spectrum). The purification was followed by measuring identity) to the sequence of the nickel-containing subunit CooH the heterodisulfide reductase activity at pH 7.5 with reduced of the hydrogenase involved in the catalysis of the energy-con-benzylviologen as electron donor (Hedderich et al, 1990) and serving carbon monoxide hydrogen lyase reaction (Eqn 5) in the H 2 -uptake hydrogenase activity at pH 7.5 with methylRhodospirillum rubrum growing anaerobically in the dark on viologen as electron donor (Heiden et al, 1993). The H 2 evolucarbon monoxide (Fox et al, 1996 a, b).…”

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An Escherichia coli hydrogenase‐3‐type hydrogenase in methanogenic archaea

Künkel

Vorholt

Thauer

et al. 1998

European Journal of Biochemistry

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102

112

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Methanogenic archaea are known to contain two types of [NiFe] hydrogenases designated F420-reducing hydrogenase and F 420 -non-reducing hydrogenase. We report here that they additionally contain Escherichia coli hydrogenase-3-type [NiFe] hydrogenases. The evidence is based on biochemical studies and analysis of the subunit primary structure of this hydrogenase (designated Ech) purified from membranes of acetate-grown cells of Methanosarcina barkeri. The subunits EchE and EchC of the EchABCDEF complex showed 34% and 45% sequence identity to the nickel-containing large subunit HycE and to the iron-sulfur cluster containing small subunit HycG, respectively, of the hydrogenase in the formate hydrogen lyase complex from E. coli. Analysis of the totally sequenced genomes of Methanococcus jannaschii and Methanobacterium thermoautotrophicum strain ∆H revealed that these organisms contain similar open reading frames, indicating the presence of an E. coli hydrogenase-3-type hydrogenase also in these methanogenic archaea.Keywords : hydrogenase ; Escherichia coli hydrogenase 3; NADH:ubiquinone oxidoreductase ; energy conservation ; Methanosarcina barkeri ; methanogenic Archaea.Most methanogenic archaea can grow on H 2 and CO 2 or The cytoplasmic enzyme is composed of three different subunits H 2 and methanol as energy sources (Wolfe, 1991; Thauer, A, β and γ and contains per A 1 , β 1 , γ 1 trimer approximately 1 mol 1997). For the activation of H 2 , they are known to contain two nickel, 1 mol FAD and several iron-sulfur clusters. The largest types of nickel hydrogenases designated coenzyme F 420-reducing A subunit harbors the dinuclear [NiFe] active site, indicated by hydrogenase and coenzyme F 420 -non-reducing hydrogenase characteristic nickel-binding motifs in the amino terminus (R-X-(Sorgenfrei et al., 1997). Both hydrogenases most probably C-X 2 -C-X 3 -H) and the carboxy terminus (D-P-C-X 2 -C-X 2 -H). Its contain nickel in a dimetallic [NiFe] reaction center (Volbeda sequence is similar to that of the large subunit of most other et Happe et al., 1997) and iron-sulfur clusters, nickel-containing hydrogenases but not to that of the large and can catalyze the reduction of viologen dyes with H 2 (Al-subunit Hyc E of the nickel hydrogenase 3 from Escherichia bracht, 1994). Some methanogenic archaea additionally contain coli (Wu and Mandrand, 1993). The γ subunit shows low sea metal-free hydrogenase designated H 2 -forming N 5 ,N 10 -methy-quence similarity to the small subunit of other [NiFe] hydrogelenetetrahydromethanopterin dehydrogenase (Thauer et al., nases. It contains a strictly conserved sequence motif 1996).CxxCx n GxCxxxGx m GCPP present in the amino-terminal region F 420 -reducing hydrogenase (Eqn 1) catalyzes the reversible of the small subunits of all [NiFe] hydrogenases sequenced thus reduction of coenzyme F 420 with H 2 to F 420 H 2 , which is obligato-far (Albracht, 1994). The crystal structure of the [NiFe] hydrorily required as electron donor in at least one step in CO 2 reduc-genase from Desulfovib...

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Section: Polypeptidementioning

confidence: 99%

Section: Polypeptidementioning

confidence: 99%

mentioning

confidence: 99%

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An Escherichia coli hydrogenase‐3‐type hydrogenase in methanogenic archaea

Künkel

Vorholt

Thauer

et al. 1998

European Journal of Biochemistry

Self Cite

102

112

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“…This membranebound, eight-subunit enzyme, encoded by the mtrECDBAFGH operon, also catalyzes the reverse, endergonic methyl transfer from methyl-CoM to H 4 SPT in the methylotrophic pathway (3). Mtr is able to drive this unfavorable methyl transfer by the consumption of the sodium ion gradient (10,11). It has been proposed that a direct methyl transfer from methanol to H 4 SPT may occur to bypass this energy-consuming step, but this has yet to be shown experimentally (12).…”

mentioning

confidence: 99%

Loss of the mtr operon in Methanosarcina blocks growth on methanol, but not methanogenesis, and reveals an unknown methanogenic pathway

Welander

Metcalf

2005

Proc. Natl. Acad. Sci. U.S.A.

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In the methanogenic archaeon Methanosarcina barkeri Fusaro, the N 5 -methyl-tetrahydrosarcinapterin (CH3-H4SPT):coenzyme M (CoM) methyltransferase, encoded by the mtr operon, catalyzes the energy-conserving (sodium-pumping) methyl transfer from CH 3-H4SPT to CoM during growth on H2͞CO2 or acetate. However, in the disproportionation of C-1 compounds, such as methanol, to methane and carbon dioxide, it catalyzes the reverse, endergonic transfer from methyl-CoM to H 4SPT, which is driven by sodium uptake. It has been proposed that a bypass for this energyconsuming reaction may occur via a direct methyl transfer from methanol to H 4SPT. To test this, an mtr deletion mutant was constructed and characterized in M. barkeri Fusaro. The mutant is unable to grow on methanol, acetate or H 2͞CO2, but can grow on methanol with H 2͞CO2 and, surprisingly, methanol with acetate. 13 C labeling experiments show that growth on acetate with methanol involves a previously unknown methanogenic pathway, in which oxidation of acetate to a mixture of CO 2 and formic acid is coupled to methanol reduction. Interestingly, although the mutant is unable to grow on methanol alone, it remains capable of producing methane from this substrate. Thus, the proposed Mtr bypass does exist, but is unable to support growth of the organism.methyltransferase ͉ mutant

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“…Thauer and coworkers detected eight di¡erent subunits in the puri¢ed enzyme by biochemical [4] and genetic analyses [5]. The dependence of the activity on sodium ions was demonstrated [6,7], the energy-conserving nature of this enzyme could not be studied because a method to generate vesicular proteosomes from Mb.…”

Section: Introductionmentioning

confidence: 99%

Cloning, sequencing and expression of the genes encoding the sodium translocating N⁵‐methyltetrahydromethanopterin:coenzyme M methyltransferase of the methylotrophic archaeon Methanosarcina mazei Gö1

Lienard

Gottschalk

1998

FEBS Letters

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The N S -methyltetrahydromethanopterin :coenzyme M methyltransferase of Methanosarcina mazei Go ë1 is a membrane-associated, corrinoid-containing protein that uses a transmethylation reaction to drive an energy-conserving sodium ion pump. The eight open reading frames encoding the eight different subunits of the methyltransferase were identified and sequenced. All of these subunits are shown to be heterologously expressed in minicells of the Escherichia coli mutant DK6. Sequence comparisons with the methyltransferases of thermophilic and hypothermophilic methanogenic archaea are presented. The participation of the gene product of mtrD in sodium ion translocation as well as a consensus sequence of a corrinoid binding motif in MtrA are discussed.z 1998 Federation of European Biochemical Societies.

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The Energy Conserving N⁵‐Methyltetrahydromethanopterin:Coenzyme M Methyltransferase Complex from Methanobacterium thermoautotrophicum is Composed of Eight Different Subunits

Cited by 71 publications

References 40 publications

An Escherichia coli hydrogenase‐3‐type hydrogenase in methanogenic archaea

An Escherichia coli hydrogenase‐3‐type hydrogenase in methanogenic archaea

Loss of the mtr operon in Methanosarcina blocks growth on methanol, but not methanogenesis, and reveals an unknown methanogenic pathway

Cloning, sequencing and expression of the genes encoding the sodium translocating N⁵‐methyltetrahydromethanopterin:coenzyme M methyltransferase of the methylotrophic archaeon Methanosarcina mazei Gö1

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The Energy Conserving N5‐Methyltetrahydromethanopterin:Coenzyme M Methyltransferase Complex from Methanobacterium thermoautotrophicum is Composed of Eight Different Subunits

Cited by 71 publications

References 40 publications

An Escherichia coli hydrogenase‐3‐type hydrogenase in methanogenic archaea

An Escherichia coli hydrogenase‐3‐type hydrogenase in methanogenic archaea

Loss of the mtr operon in Methanosarcina blocks growth on methanol, but not methanogenesis, and reveals an unknown methanogenic pathway

Cloning, sequencing and expression of the genes encoding the sodium translocating N5‐methyltetrahydromethanopterin:coenzyme M methyltransferase of the methylotrophic archaeon Methanosarcina mazei Gö1

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The Energy Conserving N⁵‐Methyltetrahydromethanopterin:Coenzyme M Methyltransferase Complex from Methanobacterium thermoautotrophicum is Composed of Eight Different Subunits

Cloning, sequencing and expression of the genes encoding the sodium translocating N⁵‐methyltetrahydromethanopterin:coenzyme M methyltransferase of the methylotrophic archaeon Methanosarcina mazei Gö1