Thermal adaptation of dihydrofolate reductase from the moderate thermophile geobacillus stearothermophilus

Guo, Jian Nan, Luk, Louis Yu Pan ORCID: https://orcid.org/0000-0002-7864-6261, Loveridge, Edric Joel and Allemann, Rudolf Konrad ORCID: https://orcid.org/0000-0002-1323-8830 2014. Thermal adaptation of dihydrofolate reductase from the moderate thermophile geobacillus stearothermophilus. Biochemistry 53 (17) , pp. 2855-2863. 10.1021/bi500238q

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Abstract

The thermal melting temperature of dihydrofolate reductase from Geobacillus stearothermophilus (BsDHFR) is 30 °C higher than that of its homologue from the psychrophile Moritella profunda. Additional proline residues in the loop regions of BsDHFR have been proposed to enhance the thermostability of BsDHFR, but site-directed mutagenesis studies reveal that these proline residues contribute only minimally. Instead, the high thermal stability of BsDHFR is partly due to removal of water-accessible thermolabile residues such as glutamine and methionine, which are prone to hydrolysis or oxidation at high temperatures. The extra thermostability of BsDHFR can be obtained by ligand binding, or in the presence of salts or cosolvents such as glycerol and sucrose. The sum of all these incremental factors allows BsDHFR to function efficiently in the natural habitat of G. stearothermophilus, which is characterized by temperatures that can reach 75 °C.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Chemistry
Subjects:	Q Science > QD Chemistry
ISSN:	0006-2960
Funders:	BBSRC
Date of First Compliant Deposit:	30 March 2016
Last Modified:	15 May 2023 17:00
URI:	https://orca.cardiff.ac.uk/id/eprint/61274

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