Exemplar Abstract for Methanothermus fervidus Stetter et al. 1982.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Kara Mannor ◽  
George M Garrity
Keyword(s):  
Methanothermus Fervidus

scholarly journals Primary structure of the heterosaccharide of the surface glycoprotein of Methanothermus fervidus.

1993 ◽  
Vol 268 (36) ◽  
pp. 26821-26826
Author(s):  
U Kärcher ◽  
H Schröder ◽  
E Haslinger ◽  
G Allmaier ◽  
R Schreiner ◽  
...  
Keyword(s):  
Primary Structure ◽  
Surface Glycoprotein ◽  
Methanothermus Fervidus

Archaeal Nucleosome Positioning Sequence from Methanothermus fervidus

1999 ◽  
Vol 289 (4) ◽  
pp. 675-681 ◽  
Author(s):  
Suzette L. Pereira ◽  
John N. Reeve
Keyword(s):  
Nucleosome Positioning ◽  
Methanothermus Fervidus

scholarly journals Complete genome sequence of Methanothermus fervidus type strain (V24ST)

2010 ◽  
Vol 3 (3) ◽  
pp. 315-324 ◽  
Author(s):  
Iain Anderson ◽  
Olivier Duplex Ngatchou Djao ◽  
Monica Misra ◽  
Olga Chertkov ◽  
Matt Nolan ◽  
...  
Keyword(s):  
Genome Sequence ◽  
Complete Genome Sequence ◽  
Complete Genome ◽  
Type Strain ◽  
Methanothermus Fervidus

scholarly journals Mutational Analysis of Differences in Thermostability between Histones from Mesophilic and Hyperthermophilic Archaea

2000 ◽  
Vol 182 (3) ◽  
pp. 812-817 ◽  
Author(s):  
Wen-Tyng Li ◽  
John W. Shriver ◽  
John N. Reeve
Keyword(s):  
Mutational Analysis ◽  
Hydrophobic Interactions ◽  
Ion Pairs ◽  
Histone Variants ◽  
Random Coil ◽  
Hyperthermophilic Archaea ◽  
Amino Acid Residues ◽  
Methanothermus Fervidus ◽  
Model Dimer ◽  
Archaeal Histone

ABSTRACT Amino acid residues responsible for the large difference in thermostability between HMfB and HFoB, archaeal histones from the hyperthermophile Methanothermus fervidus and the mesophileMethanobacterium formicicum, respectively, have been identified by site-specific mutagenesis. The thermal denaturation of ∼70 archaeal histone variants has been monitored by circular dichroism, and the data generated were fit to a two-state unfolding model (dimer→two random coil monomers) to obtain a standard-state (1M) melting temperature for each variant dimer. The results of single-, double-, and triple-residue substitutions reveal that the much higher stability of rHMfB dimers, relative to rHFoB dimers, is conferred predominantly by improved intermolecular hydrophobic interactions near the center of the histone dimer core and by additional favorable ion pairs on the dimer surface.

Genes encoding the 7S RNA and tRNASer are linked to one of the two rRNA operons in the genome of the extremely thermophilic archaebacterium Methanothermus fervidus

Gene ◽  
1990 ◽  
Vol 90 (1) ◽  
pp. 51-59 ◽  
Author(s):  
Elizabeth S. Haas ◽  
James W. Brown ◽  
Charles J. Daniels ◽  
John N. Reeve
Keyword(s):  
Genes Encoding ◽  
Methanothermus Fervidus

Hyperthermophilic dehydrogenase enzymes

2004 ◽  
Vol 32 (2) ◽  
pp. 255-258 ◽  
Author(s):  
J.A. Littlechild ◽  
J.E. Guy ◽  
M.N. Isupov
Keyword(s):  
Hydrophobic Interactions ◽  
Specific Class ◽  
Protein Chain ◽  
Salt Bridges ◽  
Sequence Identity ◽  
Dehydrogenase Enzyme ◽  
Different Types ◽  
Methanothermus Fervidus ◽  
Crystallographic Structures ◽  
Quaternary Complex

Archaeal dehydrogenases are often found to be of a specific class of dehydrogenase which has low sequence identity to the equivalent bacterial and eukaryotic counterparts. This paper focuses on two different types of hyperthermophilic dehydrogenase enzyme that have been cloned and over-expressed in Escherichia coli. The crystallographic structures of the apo form of GAPDH (glyceraldehyde-3-phosphate dehydrogenase) from Sulfolobus solfataricus and the related holo form of GAPDH from Methanothermus fervidus have been solved to high resolution. The zinc-containing structure of ADH (alcohol dehydrogenase) from Aeropyrum pernix has also been solved as a quaternary complex with the cofactor NADH and the inhibitor octanoic acid. The results show that despite the low sequence identity to the related enzymes found in other organisms the fold of the protein chain is similar. The archaeal GAPDH enzymes show a relocation of the active site which is a feature of evolutionary interest. The high thermostability of these three archaeal dehydrogenases can be attributed to a combination of factors including an increase in the number of salt bridges and hydrophobic interactions, a higher percentage of secondary structure and the presence of disulphide bonds.

scholarly journals Cloning, Sequencing, and Expression of the Gene Encoding Cyclic 2,3-Diphosphoglycerate Synthetase, the Key Enzyme of Cyclic 2,3-Diphosphoglycerate Metabolism in Methanothermus fervidus

1998 ◽  
Vol 180 (22) ◽  
pp. 5997-6004 ◽  
Author(s):  
Karl Matussek ◽  
Patrick Moritz ◽  
Nina Brunner ◽  
Christoph Eckerskorn ◽  
Reinhard Hensel
Keyword(s):  
Substrate Affinity ◽  
Kinetic Properties ◽  
Gene Encoding ◽  
Enzyme Preparations ◽  
E Coli ◽  
Gene Coding ◽  
Key Enzyme ◽  
Methanothermus Fervidus ◽  
Synthetic Reaction ◽  
Sequencing And Expression

ABSTRACT Cyclic 2,3-diphosphoglycerate synthetase (cDPGS) catalyzes the synthesis of cyclic 2,3-diphosphoglycerate (cDPG) by formation of an intramolecular phosphoanhydride bond in 2,3-diphosphoglycerate. cDPG is known to be accumulated to high intracellular concentrations (>300 mM) as a putative thermoadapter in some hyperthermophilic methanogens. For the first time, we have purified active cDPGS from a methanogen, the hyperthermophilic archaeon Methanothermus fervidus, sequenced the coding gene, and expressed it in Escherichia coli. cDPGS purification resulted in enzyme preparations containing two isoforms differing in their electrophoretic mobility under denaturing conditions. Since both polypeptides showed the same N-terminal amino acid sequence and Southern analyses indicate the presence of only one gene coding for cDPGS in M. fervidus, the two polypeptides originate from the same gene but differ by a not yet identified modification. The native cDPGS represents a dimer with an apparent molecular mass of 112 kDa and catalyzes the reversible formation of the intramolecular phosphoanhydride bond at the expense of ATP. The enzyme shows a clear preference for the synthetic reaction: the substrate affinity and the V max of the synthetic reaction are a factor of 8 to 10 higher than the corresponding values for the reverse reaction. Comparison with the kinetic properties of the electrophoretically homogeneous, apparently unmodified recombinant enzyme from E. coli revealed a twofold-higher V max of the enzyme from M. fervidus in the synthesizing direction.

NMR Structure of HMfB from the Hyperthermophile,Methanothermus fervidus, Confirms that this Archaeal Protein is a Histone

1996 ◽  
Vol 255 (1) ◽  
pp. 187-203 ◽  
Author(s):  
Mary R. Starich ◽  
Kathleen Sandman ◽  
John N. Reeve ◽  
Michael F. Summers
Keyword(s):  
Nmr Structure ◽  
Archaeal Protein ◽  
Methanothermus Fervidus
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