Sequence and structure comparison of ATP synthase F-0 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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Online Access: | http://hdl.handle.net/11577/3412315 https://doi.org/10.1371/journal.pone.0245822 |
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ftunivpadovairis:oai:www.research.unipd.it:11577/3412315 2024-04-14T08:13:20+00:00 Sequence and structure comparison of ATP synthase F-0 subunits 6 and 8 in notothenioid fish Katyal, Gunjan Ebanks, Brad Lucassen, Magnus Papetti, Chiara Chakrabarti, Lisa Katyal, Gunjan Ebanks, Brad Lucassen, Magnu Papetti, Chiara Chakrabarti, Lisa 2021 ELETTRONICO http://hdl.handle.net/11577/3412315 https://doi.org/10.1371/journal.pone.0245822 eng eng PUBLIC LIBRARY SCIENCE info:eu-repo/semantics/altIdentifier/pmid/34613983 info:eu-repo/semantics/altIdentifier/wos/WOS:000749604400004 volume:16 issue:10 firstpage:e0245822 journal:PLOS ONE http://hdl.handle.net/11577/3412315 doi:10.1371/journal.pone.0245822 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85116601844 info:eu-repo/semantics/openAccess info:eu-repo/semantics/article 2021 ftunivpadovairis https://doi.org/10.1371/journal.pone.0245822 2024-03-21T19:49:56Z 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. Article in Journal/Newspaper Icefish Padua Research Archive (IRIS - Università degli Studi di Padova) PLOS ONE 16 10 e0245822 |
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Open Polar |
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Padua Research Archive (IRIS - Università degli Studi di Padova) |
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ftunivpadovairis |
language |
English |
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. |
author2 |
Katyal, Gunjan Ebanks, Brad Lucassen, Magnu Papetti, Chiara Chakrabarti, Lisa |
format |
Article in Journal/Newspaper |
author |
Katyal, Gunjan Ebanks, Brad Lucassen, Magnus Papetti, Chiara Chakrabarti, Lisa |
spellingShingle |
Katyal, Gunjan Ebanks, Brad Lucassen, Magnus Papetti, Chiara Chakrabarti, Lisa Sequence and structure comparison of ATP synthase F-0 subunits 6 and 8 in notothenioid fish |
author_facet |
Katyal, Gunjan Ebanks, Brad Lucassen, Magnus Papetti, Chiara Chakrabarti, Lisa |
author_sort |
Katyal, Gunjan |
title |
Sequence and structure comparison of ATP synthase F-0 subunits 6 and 8 in notothenioid fish |
title_short |
Sequence and structure comparison of ATP synthase F-0 subunits 6 and 8 in notothenioid fish |
title_full |
Sequence and structure comparison of ATP synthase F-0 subunits 6 and 8 in notothenioid fish |
title_fullStr |
Sequence and structure comparison of ATP synthase F-0 subunits 6 and 8 in notothenioid fish |
title_full_unstemmed |
Sequence and structure comparison of ATP synthase F-0 subunits 6 and 8 in notothenioid fish |
title_sort |
sequence and structure comparison of atp synthase f-0 subunits 6 and 8 in notothenioid fish |
publisher |
PUBLIC LIBRARY SCIENCE |
publishDate |
2021 |
url |
http://hdl.handle.net/11577/3412315 https://doi.org/10.1371/journal.pone.0245822 |
genre |
Icefish |
genre_facet |
Icefish |
op_relation |
info:eu-repo/semantics/altIdentifier/pmid/34613983 info:eu-repo/semantics/altIdentifier/wos/WOS:000749604400004 volume:16 issue:10 firstpage:e0245822 journal:PLOS ONE http://hdl.handle.net/11577/3412315 doi:10.1371/journal.pone.0245822 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85116601844 |
op_rights |
info:eu-repo/semantics/openAccess |
op_doi |
https://doi.org/10.1371/journal.pone.0245822 |
container_title |
PLOS ONE |
container_volume |
16 |
container_issue |
10 |
container_start_page |
e0245822 |
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