Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Comparative Study
. 2011:2011:973848.
doi: 10.1155/2011/973848. Epub 2011 Apr 27.

More than 200 genes required for methane formation from H₂ and CO₂ and energy conservation are present in Methanothermobacter marburgensis and Methanothermobacter thermautotrophicus

Affiliations
Comparative Study

More than 200 genes required for methane formation from H₂ and CO₂ and energy conservation are present in Methanothermobacter marburgensis and Methanothermobacter thermautotrophicus

Anne-Kristin Kaster et al. Archaea. 2011.

Abstract

The hydrogenotrophic methanogens Methanothermobacter marburgensis and Methanothermobacter thermautotrophicus can easily be mass cultured. They have therefore been used almost exclusively to study the biochemistry of methanogenesis from H₂ and CO₂, and the genomes of these two model organisms have been sequenced. The close relationship of the two organisms is reflected in their genomic architecture and coding potential. Within the 1,607 protein coding sequences (CDS) in common, we identified approximately 200 CDS required for the synthesis of the enzymes, coenzymes, and prosthetic groups involved in CO₂ reduction to methane and in coupling this process with the phosphorylation of ADP. Approximately 20 additional genes, such as those for the biosynthesis of F(430) and methanofuran and for the posttranslational modifications of the two methyl-coenzyme M reductases, remain to be identified.

PubMed Disclaimer

Figures

Figure 1
Figure 1
Synteny between the genomes of Methanothermobacter marburgensis and Methanothermobacter thermautotrophicus. x-axis: position of CDS on the genome of M. marburgensis; y-axis: position of homologous CDS on the genome of M. thermautotrophicus. The chromosome of M. thermautotrophicus (extracted from NC_000916) was rearranged so that it starts at the corresponding CDS encoding the Cdc6 protein. Colinear similarities are depicted by red dots and anti-parallel similarities by blue dots. The synteny plot was produced by the programs of the MUMmer suite [51]. The CDS not in common are dispersed around the two genomes; many are concentrated at the four genome areas indicated by the four arrows.
Figure 2
Figure 2
Enzymes, coenzymes, and prosthetic groups involved in the energy metabolism of Methanothermobacter marburgensis and Methanothermobacter thermautotrophicus during growth on H2 and CO2. For the synthesis of these components, more than 200 coding sequences are required. A stoichiometry of 4 Na+/ATP of the A1A0-ATP synthase AhaA-IK was assumed to yield 0.5 ATP for every methane generated. This is also predicted from the thermodynamics at physiological H2 concentrations. MFR, methanofuran; H4MPT, tetrahydromethanopterin; CHO-MFR, formyl-MFR; CHO-H4MPT, formy-H4MPT; CH H4MPT+, methenyl-H4MPT+; CH2 = H4MPT, methylene-H4MPT; CH3-H4MPT, methyl-H4MPT; Fd, ferredoxin.

References

    1. Zeikus JG, Wolfe RS. Methanobacterium thermoautotrophicus Sp N, an anaerobic, autotrophic, extreme thermophile. Journal of Bacteriology. 1972;109(2):707–715. - PMC - PubMed
    1. Fuchs G, Stupperich E, Thauer RK. Acetate assimilation and the synthesis of alanine, aspartate and glutamate in Methanobacterium thermoautotrophicum . Archives of Microbiology. 1978;117(1):61–66. - PubMed
    1. DiMarco AA, Bobik TA, Wolfe RS. Unusual coenzymes of methanogenesis. Annual Review of Biochemistry. 1990;59:355–394. - PubMed
    1. Thauer RK. Biochemistry of methanogenesis: a tribute to Marjory Stephenson. Microbiology. 1998;144(9):2377–2406. - PubMed
    1. Thauer RK, Kaster AK, Goenrich M, Schick M, Hiromoto T, Shima S. Hydrogenases from methanogenic archaea, nickel, a novel cofactor, and H2 storage. Annual Review of Biochemistry. 2010;79:507–536. - PubMed

Publication types

LinkOut - more resources