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Query: UNIPROT:P06889 (Mol)
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A 5.7 kb region of chromosomal DNA from Methanothermus fervidus, harbouring a second mcr gene cluster, was cloned and sequenced. This gene cluster, termed mcrII, encodes an isoenzyme of methyl coenzyme M reductase (MCR). In contrast to the known mcr gene clusters from other methanogens, mcrII lacks mcrC, a gene of unknown function. But the remaining mcrII genes B, D, G and A are arranged in the same order as in previously sequenced mcr gene clusters. The mcrII genes from M. fervidus are located 3' to the open reading frame (ORF) B of the methylviologen-reducing hydrogenase (mvh) gene cluster. The genes of mcrII are cotranscribed, resulting in an mRNA of 4500 nucleotides. The transcriptional initiation and termination sites were identified. Phylogenetic reconstructions reveal that the mcr gene clusters fall into two different types, I and II, and that the ancestral mcr gene cluster was duplicated before the segregation of methanogens into three major orders occurred.
Mol Gen Genet 1994 Apr
PMID:Characterization and phylogeny of mcrII, a gene cluster encoding an isoenzyme of methyl coenzyme M reductase from hyperthermophilic Methanothermus fervidus. 817 16

Methanothermobacter thermautotrophicus is a thermophilic archaeon that produces methane as the end product of its primary metabolism. The biochemistry of methane formation has been extensively studied and is catalyzed by individual enzymes and proteins that are organized in protein complexes. Although much is known of the protein complexes involved in methanogenesis, only limited information is available on the associations of proteins involved in other cell processes of M. thermautotrophicus. To visualize and identify interacting and individual proteins of M. thermautotrophicus on a proteome-wide scale, protein preparations were separated using blue native electrophoresis followed by SDS-PAGE. A total of 361 proteins, corresponding to almost 20% of the predicted proteome, was identified using peptide mass fingerprinting after MALDI-TOF MS. All previously characterized complexes involved in energy generation could be visualized. Furthermore the expression and association of the heterodisulfide reductase and methylviologen-reducing hydrogenase complexes depended on culture conditions. Also homomeric supercomplexes of the ATP synthase stalk subcomplex and the N5-methyl-5,6,7,8-tetrahydromethanopterin:coenzyme M methyltransferase complex were separated. Chemical cross-linking experiments confirmed that the multimerization of both complexes was not experimentally induced. A considerable number of previously uncharacterized protein complexes were reproducibly visualized. These included an exosome-like complex consisting of four exosome core subunits, which associated with a tRNA-intron endonuclease, thereby expanding the constituency of archaeal exosomes. The results presented show the presence of novel complexes and demonstrate the added value of including blue native gel electrophoresis followed by SDS-PAGE in discovering protein complexes that are involved in catabolic, anabolic, and general cell processes.
Mol Cell Proteomics 2005 Nov
PMID:Protein complexes in the archaeon Methanothermobacter thermautotrophicus analyzed by blue native/SDS-PAGE and mass spectrometry. 1603 73