In:
Genome Research, Cold Spring Harbor Laboratory, Vol. 13, No. 7 ( 2003-07), p. 1580-1588
Abstract:
We generated draft genome sequences for two cold-adapted Archaea,
Methanogenium frigidum and Methanococcoides burtonii , to
identify genotypic characteristics that distinguish them from Archaea with a higher optimal growth temperature (OGT). Comparative genomics revealed
trends in amino acid and tRNA composition, and structural features of proteins. Proteins from the cold-adapted Archaea are characterized by
a higher content of noncharged polar amino acids, particularly Gln and Thr and a lower content of hydrophobic amino acids, particularly Leu. Sequence data
from nine methanogen genomes (OGT 15°–98°C) were used to generate 1111 modeled protein structures. Analysis of the models from the
cold-adapted Archaea showed a strong tendency in the
solvent-accessible area for more Gln, Thr, and hydrophobic residues and fewer charged residues. A cold shock domain (CSD) protein (CspA homolog) was
identified in M. frigidum , two hypothetical proteins with CSD-folds
in M. burtonii , and a unique winged helix DNA-binding domain protein
in M. burtonii . This suggests that these types of nucleic acid
binding proteins have a critical role in cold-adapted Archaea .
Structural analysis of tRNA sequences from the Archaea indicated that
GC content is the major factor influencing tRNA stability in hyperthermophiles, but not in the psychrophiles, mesophiles or moderate
thermophiles. Below an OGT of 60°C, the GC content in tRNA was largely unchanged, indicating that any requirement for flexibility of tRNA in
psychrophiles is mediated by other means. This is the first time that comparisons have been performed with genome data from Archaea spanning the growth temperature extremes from psychrophiles to
hyperthermophiles.
Type of Medium:
Online Resource
ISSN:
1088-9051
Language:
English
Publisher:
Cold Spring Harbor Laboratory
Publication Date:
2003
detail.hit.zdb_id:
1483456-X
SSG:
12
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