Pressure Adaptations in Deep-Sea <i>Moritella</i> Dihydrofolate Reductases: Compressibility versus Stability

Proteins from “pressure-loving” piezophiles appear to adapt by greater compressibility via larger total cavity volume. However, larger cavities in proteins have been associated with lower unfolding pressures. Here, dihydrofolate reductase (DHFR) from a moderate piezophile <i>Moritella profunda...

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Autores principales:	Ryan W. Penhallurick, Toshiko Ichiye
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	deep-sea adaptations compressibility cavities pressure potential energy landscape Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/3d535b27787c4d6f9c5a177425849307
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spelling	oai:doaj.org-article:3d535b27787c4d6f9c5a1774258493072021-11-25T16:48:09ZPressure Adaptations in Deep-Sea <i>Moritella</i> Dihydrofolate Reductases: Compressibility versus Stability10.3390/biology101112112079-7737https://doaj.org/article/3d535b27787c4d6f9c5a1774258493072021-11-01T00:00:00Zhttps://www.mdpi.com/2079-7737/10/11/1211https://doaj.org/toc/2079-7737Proteins from “pressure-loving” piezophiles appear to adapt by greater compressibility via larger total cavity volume. However, larger cavities in proteins have been associated with lower unfolding pressures. Here, dihydrofolate reductase (DHFR) from a moderate piezophile <i>Moritella profunda</i> (Mp) isolated at ~2.9 km in depth and from a hyperpiezophile <i>Moritella yayanosii</i> (My) isolated at ~11 km in depth were compared using molecular dynamics simulations. Although previous simulations indicate that MpDHFR is more compressible than a mesophile DHFR, here the average properties and a quasiharmonic analysis indicate that MpDHFR and MyDHFR have similar compressibilities. A cavity analysis also indicates that the three unique mutations in MyDHFR are near cavities, although the cavities are generally similar in size in both. However, while a cleft overlaps an internal cavity, thus forming a pathway from the surface to the interior in MpDHFR, the unique residue Tyr103 found in MyDHFR forms a hydrogen bond with Leu78, and the sidechain separates the cleft from the cavity. Thus, while <i>Moritella</i> DHFR may generally be well suited to high-pressure environments because of their greater compressibility, adaptation for greater depths may be to prevent water entry into the interior cavities.Ryan W. PenhallurickToshiko IchiyeMDPI AGarticledeep-sea adaptationscompressibilitycavitiespressurepotential energy landscapeBiology (General)QH301-705.5ENBiology, Vol 10, Iss 1211, p 1211 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	deep-sea adaptations compressibility cavities pressure potential energy landscape Biology (General) QH301-705.5
spellingShingle	deep-sea adaptations compressibility cavities pressure potential energy landscape Biology (General) QH301-705.5 Ryan W. Penhallurick Toshiko Ichiye Pressure Adaptations in Deep-Sea <i>Moritella</i> Dihydrofolate Reductases: Compressibility versus Stability
description	Proteins from “pressure-loving” piezophiles appear to adapt by greater compressibility via larger total cavity volume. However, larger cavities in proteins have been associated with lower unfolding pressures. Here, dihydrofolate reductase (DHFR) from a moderate piezophile <i>Moritella profunda</i> (Mp) isolated at ~2.9 km in depth and from a hyperpiezophile <i>Moritella yayanosii</i> (My) isolated at ~11 km in depth were compared using molecular dynamics simulations. Although previous simulations indicate that MpDHFR is more compressible than a mesophile DHFR, here the average properties and a quasiharmonic analysis indicate that MpDHFR and MyDHFR have similar compressibilities. A cavity analysis also indicates that the three unique mutations in MyDHFR are near cavities, although the cavities are generally similar in size in both. However, while a cleft overlaps an internal cavity, thus forming a pathway from the surface to the interior in MpDHFR, the unique residue Tyr103 found in MyDHFR forms a hydrogen bond with Leu78, and the sidechain separates the cleft from the cavity. Thus, while <i>Moritella</i> DHFR may generally be well suited to high-pressure environments because of their greater compressibility, adaptation for greater depths may be to prevent water entry into the interior cavities.
format	article
author	Ryan W. Penhallurick Toshiko Ichiye
author_facet	Ryan W. Penhallurick Toshiko Ichiye
author_sort	Ryan W. Penhallurick
title	Pressure Adaptations in Deep-Sea <i>Moritella</i> Dihydrofolate Reductases: Compressibility versus Stability
title_short	Pressure Adaptations in Deep-Sea <i>Moritella</i> Dihydrofolate Reductases: Compressibility versus Stability
title_full	Pressure Adaptations in Deep-Sea <i>Moritella</i> Dihydrofolate Reductases: Compressibility versus Stability
title_fullStr	Pressure Adaptations in Deep-Sea <i>Moritella</i> Dihydrofolate Reductases: Compressibility versus Stability
title_full_unstemmed	Pressure Adaptations in Deep-Sea <i>Moritella</i> Dihydrofolate Reductases: Compressibility versus Stability
title_sort	pressure adaptations in deep-sea <i>moritella</i> dihydrofolate reductases: compressibility versus stability
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/3d535b27787c4d6f9c5a177425849307
work_keys_str_mv	AT ryanwpenhallurick pressureadaptationsindeepseaimoritellaidihydrofolatereductasescompressibilityversusstability AT toshikoichiye pressureadaptationsindeepseaimoritellaidihydrofolatereductasescompressibilityversusstability
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Pressure Adaptations in Deep-Sea <i>Moritella</i> Dihydrofolate Reductases: Compressibility versus Stability

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