Structure and function of the globin and globin gene from the Antarctic mollusc Yoldia eightsi.

The mechanism of adaptation of haemoglobin from the Antarctic mollusc Yoldia eightsi to its low-temperature environment is a decrease in the oxygen affinity via an increased ligand-dissociation rate. At 2 degrees C this haemoglobin has an oxygen affinity similar to other haemoglobins at 25 degrees C...

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Published in:Biochemical Journal
Main Authors: Dewilde, Sylvia, Angelini, Elisa, Kiger, Laurent, Marden, Michael C, Beltramini, Mariano, Salvato, Benedetto, Moens, Luc
Format: Text
Language:English
Published: 2003
Subjects:
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1223153
http://www.ncbi.nlm.nih.gov/pubmed/12423205
https://doi.org/10.1042/BJ20020727
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spelling ftpubmed:oai:pubmedcentral.nih.gov:1223153 2023-05-15T13:42:05+02:00 Structure and function of the globin and globin gene from the Antarctic mollusc Yoldia eightsi. Dewilde, Sylvia Angelini, Elisa Kiger, Laurent Marden, Michael C Beltramini, Mariano Salvato, Benedetto Moens, Luc 2003-02-15 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1223153 http://www.ncbi.nlm.nih.gov/pubmed/12423205 https://doi.org/10.1042/BJ20020727 en eng http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1223153 http://www.ncbi.nlm.nih.gov/pubmed/12423205 http://dx.doi.org/10.1042/BJ20020727 Research Article Text 2003 ftpubmed https://doi.org/10.1042/BJ20020727 2013-08-30T14:11:13Z The mechanism of adaptation of haemoglobin from the Antarctic mollusc Yoldia eightsi to its low-temperature environment is a decrease in the oxygen affinity via an increased ligand-dissociation rate. At 2 degrees C this haemoglobin has an oxygen affinity similar to other haemoglobins at 25 degrees C. At 25 degrees C, Yoldia haemoglobin shows a low oxygen affinity, resembling that of human deoxyhaemoglobin. The mechanism involves a lower binding energy to oxygen, suggesting a loss or weakening of the usual hydrogen bond, leading to a higher oxygen-dissociation rate. However, Yoldia haemoglobin has the usual distal and proximal histidines, so the primary structure alone does not provide an obvious explanation for the low affinity. The CO-binding kinetics are biphasic, with the fraction of slow phase increasing at higher protein concentrations, indicating the formation of dimers or a higher level of polymerization. The protein-protein interaction appears to be of hydrophobic nature, since it can be partially reversed by addition of ethylene glycol as co-solvent. While the CO-association rates differ by a factor of 10, the oxygen equilibrium data could be simulated with a single affinity. The Yoldia haemoglobin gene contains three introns, interrupting the coding region at position NA1.2, B12.2 and G7.0. The conservation of the B12.2 and G7.0 introns is in contrast with the unprecedented NA1.2 intron. Phylogenetic analyses reveal a gene tree where the Yoldia haemoglobin gene is separated from other mollusc globin genes, confirming the specific adaptation of the Yoldia haemoglobin. Text Antarc* Antarctic PubMed Central (PMC) Antarctic The Antarctic Biochemical Journal 370 1 245 253
institution Open Polar
collection PubMed Central (PMC)
op_collection_id ftpubmed
language English
topic Research Article
spellingShingle Research Article
Dewilde, Sylvia
Angelini, Elisa
Kiger, Laurent
Marden, Michael C
Beltramini, Mariano
Salvato, Benedetto
Moens, Luc
Structure and function of the globin and globin gene from the Antarctic mollusc Yoldia eightsi.
topic_facet Research Article
description The mechanism of adaptation of haemoglobin from the Antarctic mollusc Yoldia eightsi to its low-temperature environment is a decrease in the oxygen affinity via an increased ligand-dissociation rate. At 2 degrees C this haemoglobin has an oxygen affinity similar to other haemoglobins at 25 degrees C. At 25 degrees C, Yoldia haemoglobin shows a low oxygen affinity, resembling that of human deoxyhaemoglobin. The mechanism involves a lower binding energy to oxygen, suggesting a loss or weakening of the usual hydrogen bond, leading to a higher oxygen-dissociation rate. However, Yoldia haemoglobin has the usual distal and proximal histidines, so the primary structure alone does not provide an obvious explanation for the low affinity. The CO-binding kinetics are biphasic, with the fraction of slow phase increasing at higher protein concentrations, indicating the formation of dimers or a higher level of polymerization. The protein-protein interaction appears to be of hydrophobic nature, since it can be partially reversed by addition of ethylene glycol as co-solvent. While the CO-association rates differ by a factor of 10, the oxygen equilibrium data could be simulated with a single affinity. The Yoldia haemoglobin gene contains three introns, interrupting the coding region at position NA1.2, B12.2 and G7.0. The conservation of the B12.2 and G7.0 introns is in contrast with the unprecedented NA1.2 intron. Phylogenetic analyses reveal a gene tree where the Yoldia haemoglobin gene is separated from other mollusc globin genes, confirming the specific adaptation of the Yoldia haemoglobin.
format Text
author Dewilde, Sylvia
Angelini, Elisa
Kiger, Laurent
Marden, Michael C
Beltramini, Mariano
Salvato, Benedetto
Moens, Luc
author_facet Dewilde, Sylvia
Angelini, Elisa
Kiger, Laurent
Marden, Michael C
Beltramini, Mariano
Salvato, Benedetto
Moens, Luc
author_sort Dewilde, Sylvia
title Structure and function of the globin and globin gene from the Antarctic mollusc Yoldia eightsi.
title_short Structure and function of the globin and globin gene from the Antarctic mollusc Yoldia eightsi.
title_full Structure and function of the globin and globin gene from the Antarctic mollusc Yoldia eightsi.
title_fullStr Structure and function of the globin and globin gene from the Antarctic mollusc Yoldia eightsi.
title_full_unstemmed Structure and function of the globin and globin gene from the Antarctic mollusc Yoldia eightsi.
title_sort structure and function of the globin and globin gene from the antarctic mollusc yoldia eightsi.
publishDate 2003
url http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1223153
http://www.ncbi.nlm.nih.gov/pubmed/12423205
https://doi.org/10.1042/BJ20020727
geographic Antarctic
The Antarctic
geographic_facet Antarctic
The Antarctic
genre Antarc*
Antarctic
genre_facet Antarc*
Antarctic
op_relation http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1223153
http://www.ncbi.nlm.nih.gov/pubmed/12423205
http://dx.doi.org/10.1042/BJ20020727
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container_title Biochemical Journal
container_volume 370
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container_start_page 245
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