Summary
Four gene clusters were identified inMethanococcus voltae which probably all encode hydrogenases of the [NiFe] type. One of these contains four genes, including those for the three subunits of the known [NiFeSe] hydrogenase capable of reducing the natural deazaflavin cofactor F420. In a second homologous cluster, the gene encoding the subunit corresponding to that which contains selenium in the know enzyme has a cysteine codon in the relevant position. In addition, two more gene clusters were detected which are very similar both in gene order and sequence to one which encodes a hydrogenase that reduces viologens inMethanobacterium thermoautotrophicum, but whose natural electron acceptor is as yet unknown. Again, in one of these clusters, one of the structural genes, which codes for a hydrogenase subunit containing the putative Ni-binding site, contains a selenocysteine codon. The homologous gene in the other clusters again shows a cysteine codon in the corresponding location. The four gene clusters are closely linked. Those encoding the two selenium-free enzymes are arranged in opposite polarities with a relatively short intergenic region. This arrangement is discussed in terms of a possible joint transcriptional regulation.
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References
Albracht SPJ, Kröger A, van der Zwaan JW, Unden G, Böcher R, Mell H, Fontijn RD (1986) Direct evidence for sulphur as a ligand to nickel in hydrogenase: an EPR study of the enzyme fromWolinella succinogenes enriched in33S. Biochim Biophys Acta 874:116–127
Alex LA, Reeve JN, Orme-Johnson WH, Walsh CT (1990) Cloning, sequence determination, and expression of the genes encoding subunits of the Ni containing 8-hydroxy-5-deazaflavin reducing hydrogenase fromMethanobacterium thermoautotrophicum ΔH. Biochemistry 29:7237–7244
Böck A, Stadtman TC (1988) Selenocysteine, a highly specific component of certain enzymes, is incorporated by a UGA-directed co -translational mechanism. Biofactors 1:245–250
Böck A, Forchhammer K, Heider J, Leinfelder W, Sawers G, Veprek B, Zinoni F (1991) Selenocysteine: the 21st amino acid. Mol Microbiol 5:515–520
Brown JW, Daniels CJ, Reeve JN (1989) Gene structure, organization and expression in archaebacteria. CRC Crit Rev Microbiol 16:287–338
Casanova JL, Pannetier C, Jaulin C, Kourilsky P (1990) Optimal conditions for directly sequencing double-stranded PCR products with Sequenase. Nucleic Acids Res 18:4028
DiMarco AA, Bobik TA, Wolfe RS (1990) Unusual coenzymes of methanogenesis. Annu Rev Biochem 59:355–394
Eidsness MK, Scott RA, Prickril BC, der Vartanian DV, LeGall J, Moura I, Moura JJG, Peck HD Jr (1989) Evidence for selenocysteine coordination to the active site nickel in the [FeNiSe] hydrogenases fromDesulfovibrio baculatus. Proc Natl Acad Sci USA 86:147–151
Erni B (1989) Glucose transport inEscherichia coli. FEMS Microbiol Rev 63:13–24
Fox JA, Livingston DJ, Orme-Johnson WH, Walsh CT (1987) 8-hydroxy-5-deazaflavin-reducing hydrogenase fromMethanobacterium thermoautotrophicum: 1. purification and characterization. Biochemistry 26:4219–4227
Frischauf AM, Lehrach H, Poustka A, Murray N (1983) Lambda replacement vectors carrying polylinker sequences. J Mol Biol 170:827–842
Grunberg-Manago M (1987) Regulation of the expression of amino-acyl-tRNA synthetases and translation factors. In: Neidhardt FD (ed)Escherichia coli andSalmonella typhimurium: Cellular and molecular biology. American Society of Microbiology, Washington, DC, pp 1386–1409
Keltjens JT, van der Drift C (1986) Electron transfer reactions in methanogens. FEMS Microbiol Rev 39:259–303
Klein A, Schnorr M (1984) Genome complexity of methanogenic bacteria. J Bacteriol 158:628–631
Klein A, Allmansberger R, Bokranz M, Knaub S, Müller B, Muth E (1988) Comparative analysis of genes encoding methyl coenzyme M reductase in methanogenic bacteria. Mol Gen Genet 213:409–420
Kothe E, Halboth S, Sitzmann J, Klein A (1990) The hydrogenase ofMethanococcus voltae: an approach to the biochemical and genetic analysis of an archaebacterial uptake hydrogenase. In: Bélaich JP, Bruschi M, Gracia JL (eds) Microbiology and biochemistry of strict anaerobes involved in interspecies hydrogen transfer. Plenum Press, New York, pp 25–36
Livingston DJ, Fox JA, Orme-Johnson WH, Walsh CT (1987) 8-Hydroxy-5-deazaflavin-reducing hydrogenase fromMethanobacterium thermoautotrophicum: 2. Kinetic and hydrogentransfer studies. Biochemistry 26:4228–4237
Muth E, Mörschel E, Klein A (1987) Purification and characterization of an 8-hydroxy-5-deazaflavin-reducing hydrogenase from the archaebacteriumMethanococcus voltae. Eur J Biochem 169:571–577
Reeve JN, Beckler GS, Cram DS, Hamilton PT, Brown JW, Krzycki JA, Kolodziej AF, Alex L, Orme-Johnson WH, Walsh CT (1989) A hydrogenase-linked gene inMethanobacterium thermoautotrophicum strain AH encodes a polyferredoxin. Proc Natl Acad Sci USA 86:3031–3035
Rospert S, Linder D, Ellermann J, Thauer RK (1990) Two genetically distinct methyl-coenzyme M reductases inMethanobacterium thermoautotrophicum strain Marburg and ΔH. Eur J Biochem 194:871–877
Saiki RK, Scharf S, Falvona F, Mullis KB, Horn GT, Erlich HA, Arnheim N (1985) Enzymatic amplification of globin genomic sequences and restriction site analysis for diagnosis of sickle cell anaemia. Science 230:1350–1354
Sambrook J, Fritsch EF, Maniatis T (1989) Molecular cloning: A laboratory manual, 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
Sanger F, Nicklen S, Coulson AR (1977) DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 74:5463–5467
Shine J, Dalgarno L (1974) The 3′-terminal sequence ofE. coli 16S rRNA: complementarity to nonsense triplets and ribosome binding sites. Proc Natl Acad Sci USA 71:1342–1346
Steigerwald VJ, Beckler GS, Reeve JN (1990) Conservation of hydrogenase and polyferredoxin structures in the hyperthermophilic archaebacteriumMethanothermus fervidus. J Bacteriol 172:4715–4718
Tinoco I, Borer PN, Dengler B, Levine MD (1973) Improved estimation of secondary structure in ribonucleic acids. Nature New Biol 246:40–41
Whitman WB, Ankwanda E, Wolfe RS (1982) Nutrition and carbon metabolism ofMethanococcus voltae. J Bacteriol 149:852–863
Whitman WB, Shieh J, Sohn S, Caras DS, Premachandran U (1986) Isolation and characterization of 22 mesophilicMethanococci. Syst Appl Microbiol 7:235–240
Zillig W, Klenk HP, Palm P, Pühler G, Gropp P, Garrett RA, Leffers H (1989) The phylogenetic relations of DNA-dependent RNA polymerases of archaebacteria, eukaryotes, and eubacteria. Can J Microbiol 35:73–80
Zinoni F, Heider J, Böck A (1990) Features of the formate dehydrogenase mRNA necessary for decoding of the UGA codon as selenocysteine. Proc Natl Acad Sci USA 87:4660–4664
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Halboth, S., Klein, A. Methanococcus voltae harbors four gene clusters potentially encoding two [NiFe] and two [NiFeSe] hydrogenases, each of the cofactor F420-reducing or F420-non-reducing types. Molec. Gen. Genet. 233, 217–224 (1992). https://doi.org/10.1007/BF00587582
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DOI: https://doi.org/10.1007/BF00587582