ArticleExtremophiles : life under extreme conditions2011
Comparative study on dihydrofolate reductases from Shewanella species living in deep-sea and ambient atmospheric-pressure environments.
Article in Extremophiles : life under extreme conditions, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 29 citations in OpenAlex.
- Pressure Adaptations in Deep-SeaBiology · 2021Article
- Adaptations for Pressure and Temperature Effects on Loop Motion inHigh pressure research · 2019Article
- Enzymes from piezophiles.Seminars in cell & developmental biology · 2018Review
- Structure-based analysis of Bacilli and plasmid dihydrofolate reductase evolution.Journal of molecular graphics & modelling · 2017Article
- Pressure adaptation of 3-isopropylmalate dehydrogenase from an extremely piezophilic bacterium is attributed to a single amino acid substitution.Extremophiles : life under extreme conditions · 2016Article
- Effects of salt on the structure, stability, and function of a halophilic dihydrofolate reductase from a hyperhalophilic archaeon, Haloarcula japonica strain TR-1.Extremophiles : life under extreme conditions · 2015Article
- Correlation between the optimal growth pressures of four Shewanella species and the stabilities of their cytochromes c 5.Extremophiles : life under extreme conditions · 2014Article
- Thermodynamic and functional characteristics of deep-sea enzymes revealed by pressure effects.Extremophiles : life under extreme conditions · 2013Review
- The role of large-scale motions in catalysis by dihydrofolate reductase.Journal of the American Chemical Society · 2011Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To examine whether dihydrofolate reductase (DHFR) from deep-sea bacteria has undergone molecular evolution to adapt to high-pressure environments, we cloned eight DHFRs from Shewanella species living in deep-sea and ambient atmospheric-pressure environments, and subsequently purified six proteins to compare their structures, stabilities, and functions. The DHFRs showed 74-90% identity in primary structure to DHFR from S. violacea, but only 55% identity to DHFR from Escherichia coli (ecDHFR). Far-ultraviolet circular dichroism and fluorescence spectra suggested that the secondary and tertiary structures of these DHFRs were similar. In addition, no significant differences were found in structural stability as monitored by urea-induced unfolding and the kinetic parameters, K(m) and k(cat); although the DHFRs from Shewanella species were less stable and more active (2- to 4-fold increases in k(cat)/K(m)) than ecDHFR. Interestingly, the pressure effects on enzyme activity revealed that DHFRs from ambient-atmospheric species are not necessarily incompatible with high pressure, and DHFRs from deep-sea species are not necessarily tolerant of high pressure. These results suggest that the DHFR molecule itself has not evolved to adapt to high-pressure environments, but rather, those Shewanella species with enzymes capable of retaining functional activity under high pressure migrated into the deep-sea.
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