Sequence and structure comparison of ATP synthase F0 subunits 6 and 8 in notothenioid fish.

Mitochondrial changes such as tight coupling of the mitochondria have facilitated sustained oxygen and respiratory activity in haemoglobin-less icefish of the Channichthyidae family. We aimed to characterise features in the sequence and structure of the proteins directly involved in proton transport...

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Autores principales:	Gunjan Katyal, Brad Ebanks, Magnus Lucassen, Chiara Papetti, Lisa Chakrabarti
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/fced3a83ba9a408c940d7ddb2a7d1774
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spelling	oai:doaj.org-article:fced3a83ba9a408c940d7ddb2a7d17742021-12-02T20:17:19ZSequence and structure comparison of ATP synthase F0 subunits 6 and 8 in notothenioid fish.1932-620310.1371/journal.pone.0245822https://doaj.org/article/fced3a83ba9a408c940d7ddb2a7d17742021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0245822https://doaj.org/toc/1932-6203Mitochondrial changes such as tight coupling of the mitochondria have facilitated sustained oxygen and respiratory activity in haemoglobin-less icefish of the Channichthyidae family. We aimed to characterise features in the sequence and structure of the proteins directly involved in proton transport, which have potential physiological implications. ATP synthase subunit a (ATP6) and subunit 8 (ATP8) are proteins that function as part of the F0 component (proton pump) of the F0F1complex. Both proteins are encoded by the mitochondrial genome and involved in oxidative phosphorylation. To explore mitochondrial sequence variation for ATP6 and ATP8 we analysed sequences from C. gunnari and C. rastrospinosus and compared them with their closely related red-blooded species and eight other vertebrate species. Our comparison of the amino acid sequence of these proteins reveals important differences that could underlie aspects of the unique physiology of the icefish. In this study we find that changes in the sequence of subunit a of the icefish C. gunnari at position 35 where there is a hydrophobic alanine which is not seen in the other notothenioids we analysed. An amino acid change of this type is significant since it may have a structural impact. The biology of the haemoglobin-less icefish is necessarily unique and any insights about these animals will help to generate a better overall understanding of important physiological pathways.Gunjan KatyalBrad EbanksMagnus LucassenChiara PapettiLisa ChakrabartiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 10, p e0245822 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Gunjan Katyal Brad Ebanks Magnus Lucassen Chiara Papetti Lisa Chakrabarti Sequence and structure comparison of ATP synthase F0 subunits 6 and 8 in notothenioid fish.
description	Mitochondrial changes such as tight coupling of the mitochondria have facilitated sustained oxygen and respiratory activity in haemoglobin-less icefish of the Channichthyidae family. We aimed to characterise features in the sequence and structure of the proteins directly involved in proton transport, which have potential physiological implications. ATP synthase subunit a (ATP6) and subunit 8 (ATP8) are proteins that function as part of the F0 component (proton pump) of the F0F1complex. Both proteins are encoded by the mitochondrial genome and involved in oxidative phosphorylation. To explore mitochondrial sequence variation for ATP6 and ATP8 we analysed sequences from C. gunnari and C. rastrospinosus and compared them with their closely related red-blooded species and eight other vertebrate species. Our comparison of the amino acid sequence of these proteins reveals important differences that could underlie aspects of the unique physiology of the icefish. In this study we find that changes in the sequence of subunit a of the icefish C. gunnari at position 35 where there is a hydrophobic alanine which is not seen in the other notothenioids we analysed. An amino acid change of this type is significant since it may have a structural impact. The biology of the haemoglobin-less icefish is necessarily unique and any insights about these animals will help to generate a better overall understanding of important physiological pathways.
format	article
author	Gunjan Katyal Brad Ebanks Magnus Lucassen Chiara Papetti Lisa Chakrabarti
author_facet	Gunjan Katyal Brad Ebanks Magnus Lucassen Chiara Papetti Lisa Chakrabarti
author_sort	Gunjan Katyal
title	Sequence and structure comparison of ATP synthase F0 subunits 6 and 8 in notothenioid fish.
title_short	Sequence and structure comparison of ATP synthase F0 subunits 6 and 8 in notothenioid fish.
title_full	Sequence and structure comparison of ATP synthase F0 subunits 6 and 8 in notothenioid fish.
title_fullStr	Sequence and structure comparison of ATP synthase F0 subunits 6 and 8 in notothenioid fish.
title_full_unstemmed	Sequence and structure comparison of ATP synthase F0 subunits 6 and 8 in notothenioid fish.
title_sort	sequence and structure comparison of atp synthase f0 subunits 6 and 8 in notothenioid fish.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/fced3a83ba9a408c940d7ddb2a7d1774
work_keys_str_mv	AT gunjankatyal sequenceandstructurecomparisonofatpsynthasef0subunits6and8innotothenioidfish AT bradebanks sequenceandstructurecomparisonofatpsynthasef0subunits6and8innotothenioidfish AT magnuslucassen sequenceandstructurecomparisonofatpsynthasef0subunits6and8innotothenioidfish AT chiarapapetti sequenceandstructurecomparisonofatpsynthasef0subunits6and8innotothenioidfish AT lisachakrabarti sequenceandstructurecomparisonofatpsynthasef0subunits6and8innotothenioidfish
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Sequence and structure comparison of ATP synthase F0 subunits 6 and 8 in notothenioid fish.

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