Mechanism of deep-sea fish α-actin pressure tolerance investigated by molecular dynamics simulations.

The pressure tolerance of monomeric α-actin proteins from the deep-sea fish Coryphaenoides armatus and C. yaquinae was compared to that of non-deep-sea fish C. acrolepis, carp, and rabbit/human/chicken actins using molecular dynamics simulations at 0.1 and 60 MPa. The amino acid sequences of actins...

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Autores principales:	Nobuhiko Wakai, Kazuhiro Takemura, Takami Morita, Akio Kitao
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/6d2325d8249f4eb49535537bf35ccac7
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spelling	oai:doaj.org-article:6d2325d8249f4eb49535537bf35ccac72021-11-18T08:37:14ZMechanism of deep-sea fish α-actin pressure tolerance investigated by molecular dynamics simulations.1932-620310.1371/journal.pone.0085852https://doaj.org/article/6d2325d8249f4eb49535537bf35ccac72014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24465747/?tool=EBIhttps://doaj.org/toc/1932-6203The pressure tolerance of monomeric α-actin proteins from the deep-sea fish Coryphaenoides armatus and C. yaquinae was compared to that of non-deep-sea fish C. acrolepis, carp, and rabbit/human/chicken actins using molecular dynamics simulations at 0.1 and 60 MPa. The amino acid sequences of actins are highly conserved across a variety of species. The actins from C. armatus and C. yaquinae have the specific substitutions Q137K/V54A and Q137K/L67P, respectively, relative to C. acrolepis, and are pressure tolerant to depths of at least 6000 m. At high pressure, we observed significant changes in the salt bridge patterns in deep-sea fish actins, and these changes are expected to stabilize ATP binding and subdomain arrangement. Salt bridges between ATP and K137, formed in deep-sea fish actins, are expected to stabilize ATP binding even at high pressure. At high pressure, deep-sea fish actins also formed a greater total number of salt bridges than non-deep-sea fish actins owing to the formation of inter-helix/strand and inter-subdomain salt bridges. Free energy analysis suggests that deep-sea fish actins are stabilized to a greater degree by the conformational energy decrease associated with pressure effect.Nobuhiko WakaiKazuhiro TakemuraTakami MoritaAkio KitaoPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 1, p e85852 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Nobuhiko Wakai Kazuhiro Takemura Takami Morita Akio Kitao Mechanism of deep-sea fish α-actin pressure tolerance investigated by molecular dynamics simulations.
description	The pressure tolerance of monomeric α-actin proteins from the deep-sea fish Coryphaenoides armatus and C. yaquinae was compared to that of non-deep-sea fish C. acrolepis, carp, and rabbit/human/chicken actins using molecular dynamics simulations at 0.1 and 60 MPa. The amino acid sequences of actins are highly conserved across a variety of species. The actins from C. armatus and C. yaquinae have the specific substitutions Q137K/V54A and Q137K/L67P, respectively, relative to C. acrolepis, and are pressure tolerant to depths of at least 6000 m. At high pressure, we observed significant changes in the salt bridge patterns in deep-sea fish actins, and these changes are expected to stabilize ATP binding and subdomain arrangement. Salt bridges between ATP and K137, formed in deep-sea fish actins, are expected to stabilize ATP binding even at high pressure. At high pressure, deep-sea fish actins also formed a greater total number of salt bridges than non-deep-sea fish actins owing to the formation of inter-helix/strand and inter-subdomain salt bridges. Free energy analysis suggests that deep-sea fish actins are stabilized to a greater degree by the conformational energy decrease associated with pressure effect.
format	article
author	Nobuhiko Wakai Kazuhiro Takemura Takami Morita Akio Kitao
author_facet	Nobuhiko Wakai Kazuhiro Takemura Takami Morita Akio Kitao
author_sort	Nobuhiko Wakai
title	Mechanism of deep-sea fish α-actin pressure tolerance investigated by molecular dynamics simulations.
title_short	Mechanism of deep-sea fish α-actin pressure tolerance investigated by molecular dynamics simulations.
title_full	Mechanism of deep-sea fish α-actin pressure tolerance investigated by molecular dynamics simulations.
title_fullStr	Mechanism of deep-sea fish α-actin pressure tolerance investigated by molecular dynamics simulations.
title_full_unstemmed	Mechanism of deep-sea fish α-actin pressure tolerance investigated by molecular dynamics simulations.
title_sort	mechanism of deep-sea fish α-actin pressure tolerance investigated by molecular dynamics simulations.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/6d2325d8249f4eb49535537bf35ccac7
work_keys_str_mv	AT nobuhikowakai mechanismofdeepseafishaactinpressuretoleranceinvestigatedbymoleculardynamicssimulations AT kazuhirotakemura mechanismofdeepseafishaactinpressuretoleranceinvestigatedbymoleculardynamicssimulations AT takamimorita mechanismofdeepseafishaactinpressuretoleranceinvestigatedbymoleculardynamicssimulations AT akiokitao mechanismofdeepseafishaactinpressuretoleranceinvestigatedbymoleculardynamicssimulations
_version_	1718421567002640384

Mechanism of deep-sea fish α-actin pressure tolerance investigated by molecular dynamics simulations.

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