Methanococcus vannielii

Jones JB, TC Stadtman (1981) Selenium-dependent and selenium-independent formate dehydrogenase of Methanococcus vannielii. Separation of the two forms and characterization of the purified selenium-independent form. J Biol Chem 256 656-663. 

DeMoll E, T Auffenberg (1993) Purine metabolism in Methanococcus vannielii J Bacterial 175 5754-5761. 

Reduction of the derivatives (76) by a selenium-containing hydrogenase from Methanococcus vannielii gave the (R)-isomers (77) as confirmed by its degradation to (78) <85PNA(82)1364>. A direct hydride equivalent transfer from C-l of alcoholates to C-5 of 5-deazaflavins was confirmed by deuteration <87JHC25i>. 

Fig. 14. Platinum-shadowed isolated S-layer of Methanococcus vannielii. From ref. [105].

It is also unclear whether archaeal mRNAs can be cotranscriptionally or post-transcriptionally modified. Polyadenylated RNAs have been identified in several archaea [21-23], the poIy(A) tails being quite short in methanogens [22] and rather long in the halophiles and the crenarchaeota [21-23]. However, evidence that they are indeed mRNAs is lacking. In any event Poly(A)+ RNAs are not capped in Methanococcus vannielii [22]. 

Abbreviations Ham, hamster Dme, Drosophila melanogaster Ddi, Dyctiostelium discoideum Sso, Sulfolobus solfataricus Pwo, Pyrococcus woesei Mva, Methanococcus vannielii Hha, Halobac-terium halobium Tac, Thermoplasma acidophilum Tma, Thermotoga maritima Tth, Thermus thermophilus Eco, Escherichia coli Mlu, Micrococcus luteus. 

Abbreviations used SS, Sulfolobus solfataricus TA, Thermoplasma acidophilum DM, Desidfuro-coccus mobilis TC, Thermococcus celer TT, Thermoproleus tenax MV, Methanococcus vannielii MF, Methanobacterium formicicum HF, Haloferax mediterranei. 

Fig. 2. The peptidyltransferase center. The structure of the central loop of Domain V of E. coli 23S rRNA is shown. Nucleotides involved in resistance against different inhibitors are indicated. Closed symbols indicate resistance and open symbols protection against chemical modification by bound antibiotic. Mutations that confer resistance to anisomycin in archaea are indicated [87] (Hcu, Halobacterium cutirubrum Hha, H. halobium). The presence of either a G or U at position 2058 in archaea is also indicated. As a consequence of this change archaea are resistant to erythromycin (Hmo, Halococcus morrhuae, Mva, Methanococcus vannielii Tte, Thermoproteus lenax Dmo, Desulfurococcus wofirfo) [29,30,88,90]. Positions where crosslinking to photoreactive derivatives of Phe-tRNA and puromycin have been observed as well as nucleotides protected by bound tRNA are also indicated. Modified from ref [73].

Some archaeal r-protein operons contain open reading frames (ORFs) that are not present in the equivalent bacterial operon. In many cases, these ORFs code for proteins which show sequence similarity to eucaryal r-proteins. For example, ORF c, d and e in the spc operon of Methanococcus vannielii [100] and Sulfolobus acidocaldarius [Kusser et al., unpublished] code for r-proteins equivalent to the eucaryal r-proteins S4 Rattus norwegicus), L32 Homo sapiens) and LI9 R. norwegicus) respectively. 

Names of organisms S.a., Sulfolobus acidocaldarius A.f, Archaeoglobus fulgidus M.f., Methano-thermus fervidus M.t., Melhanobacterium thermoautotrophicunv, M.v., Methanococcus vannielii. 

Several species have been isolated, studied in pure culture, and taxonomi-cally identified and classified. Some of the notable species are Methanobacterium formicicum, M. bryantii, M. thermoautotrophicum Methanobrevibacter ruminant-ium, M. arboriphilus, M. smithii Methanococcus vannielii, M. voltae Methanomicrobium mobile Methanogenium cariaci, M. marisnigri Methanospirillum hunga-... 

Jokela, J.K. and M. Salkinoja-Salonen. 1992. Molecular weight distributions of organic halogens in bleached kraft pulp mill effluents. Environ. Sci. Technol. 26 1190-1197. Jones, J.B. and T.C. Stadtman. 1981. Selenium-dependent and selenium-independent formate dehydrogenase of Methanococcus vannielii. Separation of the two forms and characterization of the purified selenium-independent form. J. Biol. Chem. 256 656-663. 

---