Cloning HSP70 and HSP90 genes of kaluga (Huso dauricus) and the effects of temperature and salinity stress on their gene expression.
Identifieur interne : 000094 ( Main/Exploration ); précédent : 000093; suivant : 000095Cloning HSP70 and HSP90 genes of kaluga (Huso dauricus) and the effects of temperature and salinity stress on their gene expression.
Auteurs : Guogan Peng [République populaire de Chine] ; Wen Zhao [République populaire de Chine] ; Zhenguang Shi [République populaire de Chine] ; Huirong Chen [République populaire de Chine] ; Yang Liu [République populaire de Chine] ; Jie Wei [République populaire de Chine] ; Fengying Gao [République populaire de Chine]Source :
- Cell stress & chaperones [ 1466-1268 ] ; 2016.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, Cold Temperature, Cold-Shock Response, Fish Proteins (analysis), Fish Proteins (genetics), Fishes (genetics), Fishes (physiology), Gene Expression Regulation, HSP70 Heat-Shock Proteins (analysis), HSP70 Heat-Shock Proteins (genetics), HSP90 Heat-Shock Proteins (analysis), HSP90 Heat-Shock Proteins (genetics), Phylogeny, Salinity, Stress, Physiological.
- MESH :
- chemical , analysis : Fish Proteins, HSP70 Heat-Shock Proteins, HSP90 Heat-Shock Proteins.
- chemical , genetics : Fish Proteins, HSP70 Heat-Shock Proteins, HSP90 Heat-Shock Proteins.
- genetics : Fishes.
- physiology : Fishes.
- Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, Cold Temperature, Cold-Shock Response, Gene Expression Regulation, Phylogeny, Salinity, Stress, Physiological.
Abstract
The genes encoding HSP70 and HSP90 proteins were isolated from kaluga by homologous cloning and rapid amplification of complementary DNA (cDNA) ends (RACE). HSP70 (GenBank accession no. KP050541) and HSP90 (GenBank accession no. KP050542) cDNAs were composed of 2275 and 2718 bp and encoded polypeptides of 650 and 725 amino acids, respectively. Basic Local Alignment Search Tool (BLAST) analysis showed that HSP70 and HSP90 of kaluga shared high identities with those of Acipenser ruthenus, Acipenser schrenckii, and Acipenser baerii (98-99 %). Fluorescent real-time RT-PCR under unstressed conditions revealed that HSP70 and HSP90 were expressed in 11 different tissues of kaluga. Messenger RNA (mRNA) expressions of both HSP70 and HSP90 were highest in the intestine and lowest in the muscle. In addition, the patterns of mRNA expression of HSP70 and HSP90 were similar, although the level of expression was more in HSP90 than in HSP70 (P < 0.05).We also analyzed patterns of HSP70 and HSP90 expression in the muscle, gill, and liver of kaluga under different combinations of temperature and salinity stress, including temperatures of 4,10, 25, and 28 °C at 0 ppt salinity, and salinities of 10, 20, 30, and 40 ppt at 16 °C, where 16 °C at 0 ppt (parts per thousand) served as the control. We found that levels of mRNA expression of both HSP70 and HSP90 were highest at 4 °C in the muscle, gill, and liver and changed little with salinity stress. These results increase understanding of the mechanisms of stress response of cold freshwater fish.
DOI: 10.1007/s12192-015-0665-1
PubMed: 26683614
Affiliations:
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Science, Dalian Ocean University, No.52 Heishijiao Street, Shahekou district, Dalian, 116023, Liaoning, People's Republic of China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Fisheries and Life Science, Dalian Ocean University, No.52 Heishijiao Street, Shahekou district, Dalian, 116023, Liaoning</wicri:regionArea><wicri:noRegion>Liaoning</wicri:noRegion></affiliation></author></analytic><series><title level="j">Cell stress & chaperones</title><idno type="eISSN">1466-1268</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Cloning, Molecular</term><term>Cold Temperature</term><term>Cold-Shock Response</term><term>Fish Proteins (analysis)</term><term>Fish Proteins (genetics)</term><term>Fishes (genetics)</term><term>Fishes (physiology)</term><term>Gene Expression Regulation</term><term>HSP70 Heat-Shock Proteins (analysis)</term><term>HSP70 Heat-Shock Proteins (genetics)</term><term>HSP90 Heat-Shock Proteins (analysis)</term><term>HSP90 Heat-Shock Proteins (genetics)</term><term>Phylogeny</term><term>Salinity</term><term>Stress, Physiological</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Fish Proteins</term><term>HSP70 Heat-Shock Proteins</term><term>HSP90 Heat-Shock Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fish Proteins</term><term>HSP70 Heat-Shock Proteins</term><term>HSP90 Heat-Shock Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Fishes</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Fishes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Cloning, Molecular</term><term>Cold Temperature</term><term>Cold-Shock Response</term><term>Gene Expression Regulation</term><term>Phylogeny</term><term>Salinity</term><term>Stress, Physiological</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The genes encoding HSP70 and HSP90 proteins were isolated from kaluga by homologous cloning and rapid amplification of complementary DNA (cDNA) ends (RACE). HSP70 (GenBank accession no. KP050541) and HSP90 (GenBank accession no. KP050542) cDNAs were composed of 2275 and 2718 bp and encoded polypeptides of 650 and 725 amino acids, respectively. Basic Local Alignment Search Tool (BLAST) analysis showed that HSP70 and HSP90 of kaluga shared high identities with those of Acipenser ruthenus, Acipenser schrenckii, and Acipenser baerii (98-99 %). Fluorescent real-time RT-PCR under unstressed conditions revealed that HSP70 and HSP90 were expressed in 11 different tissues of kaluga. Messenger RNA (mRNA) expressions of both HSP70 and HSP90 were highest in the intestine and lowest in the muscle. In addition, the patterns of mRNA expression of HSP70 and HSP90 were similar, although the level of expression was more in HSP90 than in HSP70 (P < 0.05).We also analyzed patterns of HSP70 and HSP90 expression in the muscle, gill, and liver of kaluga under different combinations of temperature and salinity stress, including temperatures of 4,10, 25, and 28 °C at 0 ppt salinity, and salinities of 10, 20, 30, and 40 ppt at 16 °C, where 16 °C at 0 ppt (parts per thousand) served as the control. We found that levels of mRNA expression of both HSP70 and HSP90 were highest at 4 °C in the muscle, gill, and liver and changed little with salinity stress. These results increase understanding of the mechanisms of stress response of cold freshwater fish.</div></front></TEI><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Peng, Guogan" sort="Peng, Guogan" uniqKey="Peng G" first="Guogan" last="Peng">Guogan Peng</name></noRegion><name sortKey="Chen, Huirong" sort="Chen, Huirong" uniqKey="Chen H" first="Huirong" last="Chen">Huirong Chen</name><name sortKey="Gao, Fengying" sort="Gao, Fengying" uniqKey="Gao F" first="Fengying" last="Gao">Fengying Gao</name><name sortKey="Liu, Yang" sort="Liu, Yang" uniqKey="Liu Y" first="Yang" last="Liu">Yang Liu</name><name sortKey="Shi, Zhenguang" sort="Shi, Zhenguang" uniqKey="Shi Z" first="Zhenguang" last="Shi">Zhenguang Shi</name><name sortKey="Wei, Jie" sort="Wei, Jie" uniqKey="Wei J" first="Jie" last="Wei">Jie Wei</name><name sortKey="Zhao, Wen" sort="Zhao, Wen" uniqKey="Zhao W" first="Wen" last="Zhao">Wen Zhao</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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