Methanococcus jannaschii

Graham DE, H Xu, RH White (2002) Methanococcus jannaschii uses a pyruvoyl-dependent arginine decarboxylase in polyamine biosynthesis. J Biol Chem 211 23500-23507. 

Lu ZJ, GD Markham (2004) Catalytic properties of the archaeal 5-adenosylmethionine decarboxylase from Methanococcus jannaschii. J Biol Chem 279 265-273. 

Lowe J. Crystal structure determination of FtsZ from Methanococcus jannaschii. J Struct Biol 1998 124 235-243. 

Fig. 6. Multiple alignment of a putative zinc finger in pushover/calossin and two archaeal proteins. Conserved cysteines predicted to bind Zn2+ are shown as white-on-black. Annotation of this alignment is as Fig. 4. Species abbreviations as Figs. 4 and 5, except ARCFU, Archaeoglobus fulgidus METJA, Methanococcus jannaschii.

Fig. 6. Distribution of the most common folds in selected bacterial, archaeal, and eukaryotic proteomes. The vertical axis shows the fraction of all predicted folds in the respective proteome. Fold name abbreviations FAD/NAD, FAD/NAD(P)-binding Rossman-like domains TIM, TIM-barrel domains SAM-MTR, S-adenosylmethionine-dependent methyltransferases PK, serine-threonine protein kinases PP-Loop, ATP pyrophosphatases. mge, Mycoplasma genitalium rpr, Rickettsiaprowazekii hh x, Borrelia burgdorferi ctr, Chlamydia trachomatis hpy, Helicobacter pylori tma, Thermotoga maritima ssp, Synechocystis sp. mtu, Mycobacterium tuberculosis eco, Escherichia coli mja, Methanococcus jannaschii pho, Pyrococcus horikoshii see, Saccharomyces cerevisiae, cel, Caenorhabditis elegans.

Hydrogenases (several types) Energy metabolism Methanococcus jannaschii 106... 

Figure 4 A library of Mj TyrRS mutants was generated by randomizing five residues in the tyrosine binding site. The crystai structure of Bacillus stearothermophilus TyrRS is shown with residues labeled in biack. Corresponding residues in the Methanococcus Jannaschii TyrRS are labeled in blue. Reproduced from L. Wang A. Brock B. Herberich P. G. Schultz, Science 2001, 292, 498-500, with permission from AAAS.

Bult CJ, White O, Olsen GJ, et al. 1996. Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273 1058-73. 

Figure 41 Schematic of the active site in the bifunctional inositol monophosphatase/fructose 1,6-bisphosphatase from Methanococcus jannaschii MJ109.

Sequencing of several archaeal genomes revealed the existence of genes with high sequence similarity to the ATPases of the eukaryotic 19S regulator. The deduced 50 kDa proteins have N-terminal coiled-coils, a hallmark of proteasomal AAA ATPases, and C-terminal AAA domains. The Methanococcus jannaschii protein was expressed in E. coli and purified as a 650 kD complex with nucleotidase activity. When mixed with proteasomes from Thermoplasma, degradation of substrate proteins was stimulated up to... 

T. Kawakami, R. Ohshima, T. ADP-dependent glucokinase/phosphofructo-kinase, a novel bifunctional enzyme from the hyperthermophilic archaeon Methanococcus jannaschii. J. Biol. Chem., Til, 12495-12498 (2002)... 

Selenocysteine (Sec) Selenocysteine is incorporated into a small number of proteins in species from all three kingdoms of life by a suppressor tRNASec that reads certain UGA codons, which are marked as representing selenocysteine.449 450 The selenocysteinyl-tRNA is made from a seryl-tRNA (Eq. 29-7) as described further in Chapters 16 and 24. In E. coli selenocysteine is present in three proteins, all formate dehydrogenases. The archaeon Methanococcus jannaschii contains genes for seven selenocysteine-containing proteins. Only one Sec-containing protein has been found in the nematode Caenorhabditis elegans and none in the yeast... 

Coskun, U., Chaban, Y. L., Lingl, A., Muller, V., Keegstra, W., Boekema, E. J., and Gruber, G. (2004a). Structure and subunit arrangement of the A-type ATP synthase complex from the archaeon Methanococcus jannaschii visualized by electron microscopy./. Biol. Chem. 279, 38644-38648. 

Bult CJ, White O, Olsen GJ, Zhou L, Fleischmann RD, Sutton GG et al (1996) Complete genome sequence of the methanogenic archaeon Methanococcus jannaschii. Science 273 1058-1072 Canback B, Andersson SGE, Kurland CG (2002) The global phylogeny of glycolytic enzymes. Proc Natl Acad Sci USA 99 6097-6102... 

A thermostable dimer was therefore considered as an alternative starting point for the design of a stable monomeric mutase. A large number of EcCM sequence homo-logues, some from thermophilic organisms, are known. For example, the hyperther-mophilic archaeon Methanococcus jannaschii produces a chorismate mutase (MjCM) that is 25 °C more stable than EcCM [37]. Despite only 21 % sequence identity, six prominent residues that line the active site are strictly conserved and the two enzymes have comparable activities. Since the hydrophobic core of MjCM is very similar to that of EcCM, interactions distant from the dimer interface must be responsible for its additional stability. These same interactions were expected to stabilize the desired monomer. 

Chen, L., and Roberts, M.F., 1998, Cloning and expression of the inositol monophosphatase gene from Methanococcus jannaschii and characterization of the enzyme. Appl. Environ. Microbiol. 64 2609-2615. 

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