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°C this haemoglobin has an oxygen affinity similar to other haemoglobins at 25°C. At 25°C, Yoldi...
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crportlandpress:10.1042/bj20020727 2024-06-09T07:41:09+00:00 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 http://dx.doi.org/10.1042/bj20020727 https://portlandpress.com/biochemj/article-pdf/370/1/245/710592/bj3700245.pdf en eng Portland Press Ltd. Biochemical Journal volume 370, issue 1, page 245-253 ISSN 0264-6021 1470-8728 journal-article 2003 crportlandpress https://doi.org/10.1042/bj20020727 2024-05-16T14:10:08Z 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°C this haemoglobin has an oxygen affinity similar to other haemoglobins at 25°C. At 25°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. Article in Journal/Newspaper Antarc* Antarctic Portland Press Antarctic The Antarctic Biochemical Journal 370 1 245 253 |
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Portland Press |
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English |
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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°C this haemoglobin has an oxygen affinity similar to other haemoglobins at 25°C. At 25°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 |
Article in Journal/Newspaper |
author |
DEWILDE, Sylvia ANGELINI, Elisa KIGER, Laurent MARDEN, Michael C. BELTRAMINI, Mariano SALVATO, Benedetto MOENS, Luc |
spellingShingle |
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 |
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 |
publisher |
Portland Press Ltd. |
publishDate |
2003 |
url |
http://dx.doi.org/10.1042/bj20020727 https://portlandpress.com/biochemj/article-pdf/370/1/245/710592/bj3700245.pdf |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Biochemical Journal volume 370, issue 1, page 245-253 ISSN 0264-6021 1470-8728 |
op_doi |
https://doi.org/10.1042/bj20020727 |
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Biochemical Journal |
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370 |
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1 |
container_start_page |
245 |
op_container_end_page |
253 |
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1801369581541916672 |