The adaptive evolution of polar fishes: Structure, function and molecular phylogeny of hemoglobin

emperature affects all molecular processes and is the major determinant of habitat suitability. Whilst there is an increasing understanding of evolutionary adaptation to temperature in some processes, several key questions often remain open about the structure-function relationships associated with...

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Main Authors: Verde, Cinzia, Di Prisco, Guido
Format: Report
Language:English
Published: Institute of Protein Biochemistry, C.N.R./Institute of Protein Biochemistry, C.N.R. 2006
Subjects:
Online Access:https://nipr.repo.nii.ac.jp/?action=repository_uri&item_id=2506
http://id.nii.ac.jp/1291/00002506/
https://nipr.repo.nii.ac.jp/?action=repository_action_common_download&item_id=2506&item_no=1&attribute_id=18&file_no=1
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spelling ftnipr:oai:nipr.repo.nii.ac.jp:00002506 2023-05-15T13:48:00+02:00 The adaptive evolution of polar fishes: Structure, function and molecular phylogeny of hemoglobin Verde, Cinzia Di Prisco, Guido 2006-03 https://nipr.repo.nii.ac.jp/?action=repository_uri&item_id=2506 http://id.nii.ac.jp/1291/00002506/ https://nipr.repo.nii.ac.jp/?action=repository_action_common_download&item_id=2506&item_no=1&attribute_id=18&file_no=1 en eng Institute of Protein Biochemistry, C.N.R./Institute of Protein Biochemistry, C.N.R. https://nipr.repo.nii.ac.jp/?action=repository_uri&item_id=2506 http://id.nii.ac.jp/1291/00002506/ AA00733561 Memoirs of National Institute of Polar Research. Special issue, 59, 16-28(2006-03) https://nipr.repo.nii.ac.jp/?action=repository_action_common_download&item_id=2506&item_no=1&attribute_id=18&file_no=1 polar fish hemoglobin molecular phylogeny Departmental Bulletin Paper P(論文) 2006 ftnipr 2022-11-12T19:43:20Z emperature affects all molecular processes and is the major determinant of habitat suitability. Whilst there is an increasing understanding of evolutionary adaptation to temperature in some processes, several key questions often remain open about the structure-function relationships associated with protein thermal adaptation. Proteins, such as hemoglobin, are highly sensitive to temperature and therefore, their structural and functional properties mirror the thermal conditions encountered by species during their evolutionary histories. The most stable thermal environments are aquatic; research on polar fishes has provided important insights into the details of thermal adaptation. In polar fishes, the evolution of hemoglobin includes adaptations with implications at the biochemical, physiological and structural levels. Although both are cold, the Northern and Southern polar oceans have very different oceanographic features. In comparison with Antarctic fish of the suborder Notothenioidei, Arctic fish are characterised by higher biodiversity and hemoglobin multiplicity. Within the study of the molecular bases of cold adaptation in fish inhabiting the polar habitats, and taking advantage of the information available on hemoglobin structure and function, the evolutionary history of the α and β globins of Arctic and Antarctic fish hemoglobins has been analysed, under the assumption of the molecular-clock hypothesis. Report Antarc* Antarctic Arctic Memoirs of National Institute of Polar Research Polar Research National Institute of Polar Research Repository, Japan Antarctic Arctic
institution Open Polar
collection National Institute of Polar Research Repository, Japan
op_collection_id ftnipr
language English
topic polar fish
hemoglobin
molecular phylogeny
spellingShingle polar fish
hemoglobin
molecular phylogeny
Verde, Cinzia
Di Prisco, Guido
The adaptive evolution of polar fishes: Structure, function and molecular phylogeny of hemoglobin
topic_facet polar fish
hemoglobin
molecular phylogeny
description emperature affects all molecular processes and is the major determinant of habitat suitability. Whilst there is an increasing understanding of evolutionary adaptation to temperature in some processes, several key questions often remain open about the structure-function relationships associated with protein thermal adaptation. Proteins, such as hemoglobin, are highly sensitive to temperature and therefore, their structural and functional properties mirror the thermal conditions encountered by species during their evolutionary histories. The most stable thermal environments are aquatic; research on polar fishes has provided important insights into the details of thermal adaptation. In polar fishes, the evolution of hemoglobin includes adaptations with implications at the biochemical, physiological and structural levels. Although both are cold, the Northern and Southern polar oceans have very different oceanographic features. In comparison with Antarctic fish of the suborder Notothenioidei, Arctic fish are characterised by higher biodiversity and hemoglobin multiplicity. Within the study of the molecular bases of cold adaptation in fish inhabiting the polar habitats, and taking advantage of the information available on hemoglobin structure and function, the evolutionary history of the α and β globins of Arctic and Antarctic fish hemoglobins has been analysed, under the assumption of the molecular-clock hypothesis.
format Report
author Verde, Cinzia
Di Prisco, Guido
author_facet Verde, Cinzia
Di Prisco, Guido
author_sort Verde, Cinzia
title The adaptive evolution of polar fishes: Structure, function and molecular phylogeny of hemoglobin
title_short The adaptive evolution of polar fishes: Structure, function and molecular phylogeny of hemoglobin
title_full The adaptive evolution of polar fishes: Structure, function and molecular phylogeny of hemoglobin
title_fullStr The adaptive evolution of polar fishes: Structure, function and molecular phylogeny of hemoglobin
title_full_unstemmed The adaptive evolution of polar fishes: Structure, function and molecular phylogeny of hemoglobin
title_sort adaptive evolution of polar fishes: structure, function and molecular phylogeny of hemoglobin
publisher Institute of Protein Biochemistry, C.N.R./Institute of Protein Biochemistry, C.N.R.
publishDate 2006
url https://nipr.repo.nii.ac.jp/?action=repository_uri&item_id=2506
http://id.nii.ac.jp/1291/00002506/
https://nipr.repo.nii.ac.jp/?action=repository_action_common_download&item_id=2506&item_no=1&attribute_id=18&file_no=1
geographic Antarctic
Arctic
geographic_facet Antarctic
Arctic
genre Antarc*
Antarctic
Arctic
Memoirs of National Institute of Polar Research
Polar Research
genre_facet Antarc*
Antarctic
Arctic
Memoirs of National Institute of Polar Research
Polar Research
op_relation https://nipr.repo.nii.ac.jp/?action=repository_uri&item_id=2506
http://id.nii.ac.jp/1291/00002506/
AA00733561
Memoirs of National Institute of Polar Research. Special issue, 59, 16-28(2006-03)
https://nipr.repo.nii.ac.jp/?action=repository_action_common_download&item_id=2506&item_no=1&attribute_id=18&file_no=1
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