Tilapia and human CLIC2 structures are highly conserved.
Identifieur interne : 000200 ( Main/Exploration ); précédent : 000199; suivant : 000201Tilapia and human CLIC2 structures are highly conserved.
Auteurs : Jiao Zeng [Singapour] ; Zhengjun Li [Singapour] ; Eei Yin Lui [Singapour] ; Siew Hong Lam [Singapour] ; Kunchithapadam Swaminathan [Singapour]Source :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2018.
Descripteurs français
- KwdFr :
- ARN messager (génétique), ARN messager (métabolisme), Animaux (MeSH), Canaux chlorure (composition chimique), Canaux chlorure (génétique), Canaux chlorure (métabolisme), Conformation des protéines (MeSH), Humains (MeSH), Modèles moléculaires (MeSH), Osmorégulation (génétique), Osmorégulation (physiologie), Phylogenèse (MeSH), Protéines de poisson (composition chimique), Protéines de poisson (génétique), Protéines de poisson (métabolisme), Salinité (MeSH), Similitude de séquences d'acides aminés (MeSH), Séquence conservée (MeSH), Séquence d'acides aminés (MeSH), Tilapia (génétique), Tilapia (physiologie).
- MESH :
- composition chimique : Canaux chlorure, Protéines de poisson.
- génétique : ARN messager, Canaux chlorure, Osmorégulation, Protéines de poisson, Tilapia.
- métabolisme : ARN messager, Canaux chlorure, Protéines de poisson.
- physiologie : Osmorégulation, Tilapia.
- Animaux, Conformation des protéines, Humains, Modèles moléculaires, Phylogenèse, Salinité, Similitude de séquences d'acides aminés, Séquence conservée, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Chloride Channels (chemistry), Chloride Channels (genetics), Chloride Channels (metabolism), Conserved Sequence (MeSH), Fish Proteins (chemistry), Fish Proteins (genetics), Fish Proteins (metabolism), Humans (MeSH), Models, Molecular (MeSH), Osmoregulation (genetics), Osmoregulation (physiology), Phylogeny (MeSH), Protein Conformation (MeSH), RNA, Messenger (genetics), RNA, Messenger (metabolism), Salinity (MeSH), Sequence Homology, Amino Acid (MeSH), Tilapia (genetics), Tilapia (physiology).
- MESH :
- chemical , chemistry : Chloride Channels, Fish Proteins.
- chemical , genetics : Chloride Channels, Fish Proteins, RNA, Messenger.
- chemical , metabolism : Chloride Channels, Fish Proteins, RNA, Messenger.
- genetics : Osmoregulation, Tilapia.
- physiology : Osmoregulation, Tilapia.
- Amino Acid Sequence, Animals, Conserved Sequence, Humans, Models, Molecular, Phylogeny, Protein Conformation, Salinity, Sequence Homology, Amino Acid.
Abstract
Chloride intracellular channels (CLICs) exist in soluble and membrane bound forms. We have determined the crystal structure of soluble Clic2 from the euryhaline teleost fish Oreochromis mossambicus. Structural comparison of tilapia and human CLIC2 with other CLICs shows that these proteins are highly conserved. We have also compared the expression levels of clic2 in selected osmoregulatory organs of tilapia, acclimated to freshwater, seawater and hypersaline water. Structural conservation of vertebrate CLICs implies that they might play conserved roles. Also, tissue-specific responsiveness of clic2 suggests that it might be involved in iono-osmoregulation under extreme conditions in tilapia.
DOI: 10.1016/j.bbrc.2017.11.189
PubMed: 29198705
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<term>Chloride Channels (genetics)</term>
<term>Chloride Channels (metabolism)</term>
<term>Conserved Sequence (MeSH)</term>
<term>Fish Proteins (chemistry)</term>
<term>Fish Proteins (genetics)</term>
<term>Fish Proteins (metabolism)</term>
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<term>Models, Molecular (MeSH)</term>
<term>Osmoregulation (genetics)</term>
<term>Osmoregulation (physiology)</term>
<term>Phylogeny (MeSH)</term>
<term>Protein Conformation (MeSH)</term>
<term>RNA, Messenger (genetics)</term>
<term>RNA, Messenger (metabolism)</term>
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<term>Tilapia (physiology)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>ARN messager (génétique)</term>
<term>ARN messager (métabolisme)</term>
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<term>Canaux chlorure (composition chimique)</term>
<term>Canaux chlorure (génétique)</term>
<term>Canaux chlorure (métabolisme)</term>
<term>Conformation des protéines (MeSH)</term>
<term>Humains (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
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<term>Osmorégulation (physiologie)</term>
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<term>Protéines de poisson (métabolisme)</term>
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<term>Tilapia (physiologie)</term>
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<term>RNA, Messenger</term>
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<term>Protéines de poisson</term>
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<term>Tilapia</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ARN messager</term>
<term>Canaux chlorure</term>
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<term>Protéines de poisson</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN messager</term>
<term>Canaux chlorure</term>
<term>Protéines de poisson</term>
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<term>Tilapia</term>
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<term>Animals</term>
<term>Conserved Sequence</term>
<term>Humans</term>
<term>Models, Molecular</term>
<term>Phylogeny</term>
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<term>Salinity</term>
<term>Sequence Homology, Amino Acid</term>
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<term>Conformation des protéines</term>
<term>Humains</term>
<term>Modèles moléculaires</term>
<term>Phylogenèse</term>
<term>Salinité</term>
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<front><div type="abstract" xml:lang="en">Chloride intracellular channels (CLICs) exist in soluble and membrane bound forms. We have determined the crystal structure of soluble Clic2 from the euryhaline teleost fish Oreochromis mossambicus. Structural comparison of tilapia and human CLIC2 with other CLICs shows that these proteins are highly conserved. We have also compared the expression levels of clic2 in selected osmoregulatory organs of tilapia, acclimated to freshwater, seawater and hypersaline water. Structural conservation of vertebrate CLICs implies that they might play conserved roles. Also, tissue-specific responsiveness of clic2 suggests that it might be involved in iono-osmoregulation under extreme conditions in tilapia.</div>
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<Abstract><AbstractText>Chloride intracellular channels (CLICs) exist in soluble and membrane bound forms. We have determined the crystal structure of soluble Clic2 from the euryhaline teleost fish Oreochromis mossambicus. Structural comparison of tilapia and human CLIC2 with other CLICs shows that these proteins are highly conserved. We have also compared the expression levels of clic2 in selected osmoregulatory organs of tilapia, acclimated to freshwater, seawater and hypersaline water. Structural conservation of vertebrate CLICs implies that they might play conserved roles. Also, tissue-specific responsiveness of clic2 suggests that it might be involved in iono-osmoregulation under extreme conditions in tilapia.</AbstractText>
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<name sortKey="Lui, Eei Yin" sort="Lui, Eei Yin" uniqKey="Lui E" first="Eei Yin" last="Lui">Eei Yin Lui</name>
<name sortKey="Swaminathan, Kunchithapadam" sort="Swaminathan, Kunchithapadam" uniqKey="Swaminathan K" first="Kunchithapadam" last="Swaminathan">Kunchithapadam Swaminathan</name>
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