NDLI: Methionine Sulfoxide Reductase from the Hyperthermophilic Archaeon Thermococcus kodakaraensis, an Enzyme Designed To Function at Suboptimal Growth Temperatures▿

Content Provider	PubMed Central
Author	Fukushima, Eiji Shinka, Yasuhiro Fukui, Toshiaki Atomi, Haruyuki Imanaka, Tadayuki
Copyright Year	2007
Abstract	Methionine sulfoxide reductase (Msr) catalyzes the thioredoxin-dependent reduction and repair of methionine sulfoxide (MetO). Although Msr genes are not present in most hyperthermophile genomes, an Msr homolog encoding an MsrA-MsrB fusion protein (MsrABTk) was present on the genome of the hyperthermophilic archaeon Thermococcus kodakaraensis. Recombinant proteins corresponding to MsrABTk and the individual domains (MsrATk and MsrBTk) were produced, purified, and biochemically examined. MsrATk and MsrBTk displayed strict substrate selectivity for Met-S-O and Met-R-O, respectively. MsrABTk, and in particular the MsrB domain of this protein, displayed an intriguing behavior for an enzyme from a hyperthermophile. While MsrABTk was relatively stable at temperatures up to 80°C (with a half-life of ∼30 min at 80°C), a 75% decrease in activity was observed after 2.5 min at 85°C, the optimal growth temperature of this archaeon. Moreover, maximal levels of MsrB activity of MsrABTk were observed at the strikingly low temperature of 30°C, which also was observed for MsrBTk. Consistent with the low-temperature-specific biochemical properties of MsrABTk, the presence of the protein was greater in T. kodakaraensis cells grown at suboptimal temperatures (60 to 70°C) and could not be detected at 80 to 90°C. We found that the amount of intracellular MsrABTk protein increased with exposure to higher dissolved oxygen levels, but only at suboptimal growth temperatures. While measuring background rates of the Msr enzyme reactions, we observed significant levels of MetO reduction at high temperatures without enzyme. The occurrence of nonenzymatic MetO reduction at high temperatures may explain the specific absence of Msr homologs in most hyperthermophiles. Together with the fact that the presence of Msr in T. kodakaraensis is exceptional among the hyperthermophiles, the enzyme may represent a novel strategy for this organism to deal with low-temperature environments in which the dissolved oxygen concentrations increase.
Related Links	http://dx.doi.org/10.1128/JB.00751-06
Starting Page	7134
File Format	PDF
ISSN	10985530
e-ISSN	10985530
Journal	Journal of Bacteriology
Issue Number	19
Volume Number	189
Language	English
Publisher	American Society for Microbiology
Publisher Date	2007-10-01
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Microbiology

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