Molecular Biology and Evolution, Vol 16, 1785-1790, Copyright © 1999 by Society for Molecular Biology and Evolution
JH McDonald, AM Grasso and LK Rejto
It has long been known that amino acid substitutions in proteins of
organisms living at moderate and high temperatures (mesophiles and
thermophiles, respectively) are not all symmetrical; for example, more
aligned sites have lysine in mesophiles and arginine in thermophiles than
have the opposite pattern. This is generally taken to indicate that certain
amino acids are favored over others by selection at different temperatures.
Previous comparisons of protein sequences from mesophiles and thermophiles
have used relatively small numbers of sequences from a diverse array of
species, meaning that only the most common amino acid substitutions could
be examined and any taxon- specific patterns would be obscured. Here, we
compare a large number of proteins between mesophiles and thermophiles in
the archaeal genus Methanococcus and the bacterial genus Bacillus. Each
genus exhibits dramatically asymmetrical substitution patterns for many
pairs of amino acids. There are several pairs of amino acids for which one
amino acid is favored in thermophilic Bacillus and the other is favored in
thermophilic Methanococcus; this appears to result from the higher G + C
content of the DNA of thermophilic Bacillus, a complication not seen in
Methanococcus.
ORIGINAL ARTICLE
Patterns of temperature adaptation in proteins from Methanococcus and Bacillus
Department of Biological Sciences, University of Delaware, Newwark 19716, USA. mcdonald@udel.edu
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