Functional analysis of the Na+,K+/H+ antiporter PeNHX3 from the tree halophyte Populus euphratica in yeast by model-guided mutagenesis.
Identifieur interne : 002221 ( Main/Exploration ); précédent : 002220; suivant : 002222Functional analysis of the Na+,K+/H+ antiporter PeNHX3 from the tree halophyte Populus euphratica in yeast by model-guided mutagenesis.
Auteurs : Liguang Wang [République populaire de Chine] ; Xueying Feng [République populaire de Chine] ; Hong Zhao [République populaire de Chine] ; Lidong Wang [République populaire de Chine] ; Lizhe An [République populaire de Chine] ; Quan-Sheng Qiu [République populaire de Chine]Source :
- PloS one [ 1932-6203 ] ; 2014.
Descripteurs français
- KwdFr :
- Antiport des ions sodium-hydrogène (composition chimique), Antiport des ions sodium-hydrogène (métabolisme), Arbres (métabolisme), Données de séquences moléculaires (MeSH), Escherichia coli (métabolisme), Interactions hydrophobes et hydrophiles (MeSH), Lithium (métabolisme), Modèles moléculaires (MeSH), Motifs d'acides aminés (MeSH), Mutagenèse (MeSH), Plantes tolérantes au sel (métabolisme), Populus (métabolisme), Potassium (métabolisme), Protéines Escherichia coli (composition chimique), Protéines végétales (composition chimique), Relation structure-activité (MeSH), Saccharomyces cerevisiae (métabolisme), Sodium (métabolisme), Structure secondaire des protéines (MeSH), Structure tertiaire des protéines (MeSH), Séquence conservée (MeSH), Séquence d'acides aminés (MeSH), Transport biologique (MeSH).
- MESH :
- composition chimique : Antiport des ions sodium-hydrogène, Protéines Escherichia coli, Protéines végétales.
- métabolisme : Antiport des ions sodium-hydrogène, Arbres, Escherichia coli, Lithium, Plantes tolérantes au sel, Populus, Potassium, Saccharomyces cerevisiae, Sodium.
- Données de séquences moléculaires, Interactions hydrophobes et hydrophiles, Modèles moléculaires, Motifs d'acides aminés, Mutagenèse, Relation structure-activité, Structure secondaire des protéines, Structure tertiaire des protéines, Séquence conservée, Séquence d'acides aminés, Transport biologique.
English descriptors
- KwdEn :
- Amino Acid Motifs (MeSH), Amino Acid Sequence (MeSH), Biological Transport (MeSH), Conserved Sequence (MeSH), Escherichia coli (metabolism), Escherichia coli Proteins (chemistry), Hydrophobic and Hydrophilic Interactions (MeSH), Lithium (metabolism), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Mutagenesis (MeSH), Plant Proteins (chemistry), Populus (metabolism), Potassium (metabolism), Protein Structure, Secondary (MeSH), Protein Structure, Tertiary (MeSH), Saccharomyces cerevisiae (metabolism), Salt-Tolerant Plants (metabolism), Sodium (metabolism), Sodium-Hydrogen Exchangers (chemistry), Sodium-Hydrogen Exchangers (metabolism), Structure-Activity Relationship (MeSH), Trees (metabolism).
- MESH :
- chemical , chemistry : Escherichia coli Proteins, Plant Proteins, Sodium-Hydrogen Exchangers.
- metabolism : Escherichia coli, Lithium, Populus, Potassium, Saccharomyces cerevisiae, Salt-Tolerant Plants, Sodium, Sodium-Hydrogen Exchangers, Trees.
- Amino Acid Motifs, Amino Acid Sequence, Biological Transport, Conserved Sequence, Hydrophobic and Hydrophilic Interactions, Models, Molecular, Molecular Sequence Data, Mutagenesis, Protein Structure, Secondary, Protein Structure, Tertiary, Structure-Activity Relationship.
Abstract
Na+,K+/H+ antiporters are H+-coupled cotransporters that are crucial for cellular homeostasis. Populus euphratica, a well-known tree halophyte, contains six Na+/H+ antiporter genes (PeNHX1-6) that have been shown to function in salt tolerance. However, the catalytic mechanisms governing their ion transport remain largely unknown. Using the crystal structure of the Na+/H+ antiporter from the Escherichia coli (EcNhaA) as a template, we built the three-dimensional structure of PeNHX3 from P. euphratica. The PeNHX3 model displays the typical TM4-TM11 assembly that is critical for ion binding and translocation. The PeNHX3 structure follows the 'positive-inside' rule and exhibits a typical physicochemical property of the transporter proteins. Four conserved residues, including Tyr149, Asn187, Asp188, and Arg356, are indentified in the TM4-TM11 assembly region of PeNHX3. Mutagenesis analysis showed that these reserved residues were essential for the function of PeNHX3: Asn187 and Asp188 (forming a ND motif) controlled ion binding and translocation, and Tyr149 and Arg356 compensated helix dipoles in the TM4-TM11 assembly. PeNHX3 mediated Na+, K+ and Li+ transport in a yeast growth assay. Domain-switch analysis shows that TM11 is crucial to Li+ transport. The novel features of PeNHX3 in ion binding and translocation are discussed.
DOI: 10.1371/journal.pone.0104147
PubMed: 25093858
PubMed Central: PMC4122410
Affiliations:
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(MeSH)</term><term>Mutagenesis (MeSH)</term><term>Plant Proteins (chemistry)</term><term>Populus (metabolism)</term><term>Potassium (metabolism)</term><term>Protein Structure, Secondary (MeSH)</term><term>Protein Structure, Tertiary (MeSH)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Salt-Tolerant Plants (metabolism)</term><term>Sodium (metabolism)</term><term>Sodium-Hydrogen Exchangers (chemistry)</term><term>Sodium-Hydrogen Exchangers (metabolism)</term><term>Structure-Activity Relationship (MeSH)</term><term>Trees (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antiport des ions sodium-hydrogène (composition chimique)</term><term>Antiport des ions sodium-hydrogène (métabolisme)</term><term>Arbres (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (métabolisme)</term><term>Interactions hydrophobes et hydrophiles (MeSH)</term><term>Lithium (métabolisme)</term><term>Modèles moléculaires (MeSH)</term><term>Motifs d'acides aminés (MeSH)</term><term>Mutagenèse (MeSH)</term><term>Plantes tolérantes au sel (métabolisme)</term><term>Populus (métabolisme)</term><term>Potassium (métabolisme)</term><term>Protéines Escherichia coli (composition chimique)</term><term>Protéines végétales (composition chimique)</term><term>Relation structure-activité (MeSH)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Sodium (métabolisme)</term><term>Structure secondaire des protéines (MeSH)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Séquence conservée (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Transport biologique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Escherichia coli Proteins</term><term>Plant Proteins</term><term>Sodium-Hydrogen Exchangers</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Antiport des ions sodium-hydrogène</term><term>Protéines Escherichia coli</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term><term>Lithium</term><term>Populus</term><term>Potassium</term><term>Saccharomyces cerevisiae</term><term>Salt-Tolerant Plants</term><term>Sodium</term><term>Sodium-Hydrogen Exchangers</term><term>Trees</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antiport des ions sodium-hydrogène</term><term>Arbres</term><term>Escherichia coli</term><term>Lithium</term><term>Plantes tolérantes au sel</term><term>Populus</term><term>Potassium</term><term>Saccharomyces cerevisiae</term><term>Sodium</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Biological Transport</term><term>Conserved Sequence</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Mutagenesis</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Données de séquences moléculaires</term><term>Interactions hydrophobes et hydrophiles</term><term>Modèles moléculaires</term><term>Motifs d'acides aminés</term><term>Mutagenèse</term><term>Relation structure-activité</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Séquence conservée</term><term>Séquence d'acides aminés</term><term>Transport biologique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Na+,K+/H+ antiporters are H+-coupled cotransporters that are crucial for cellular homeostasis. Populus euphratica, a well-known tree halophyte, contains six Na+/H+ antiporter genes (PeNHX1-6) that have been shown to function in salt tolerance. However, the catalytic mechanisms governing their ion transport remain largely unknown. Using the crystal structure of the Na+/H+ antiporter from the Escherichia coli (EcNhaA) as a template, we built the three-dimensional structure of PeNHX3 from P. euphratica. The PeNHX3 model displays the typical TM4-TM11 assembly that is critical for ion binding and translocation. The PeNHX3 structure follows the 'positive-inside' rule and exhibits a typical physicochemical property of the transporter proteins. Four conserved residues, including Tyr149, Asn187, Asp188, and Arg356, are indentified in the TM4-TM11 assembly region of PeNHX3. Mutagenesis analysis showed that these reserved residues were essential for the function of PeNHX3: Asn187 and Asp188 (forming a ND motif) controlled ion binding and translocation, and Tyr149 and Arg356 compensated helix dipoles in the TM4-TM11 assembly. PeNHX3 mediated Na+, K+ and Li+ transport in a yeast growth assay. Domain-switch analysis shows that TM11 is crucial to Li+ transport. The novel features of PeNHX3 in ion binding and translocation are discussed. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25093858</PMID><DateCompleted><Year>2015</Year><Month>11</Month><Day>10</Day></DateCompleted><DateRevised><Year>2019</Year><Month>02</Month><Day>23</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>9</Volume><Issue>8</Issue><PubDate><Year>2014</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS One</ISOAbbreviation></Journal><ArticleTitle>Functional analysis of the Na+,K+/H+ antiporter PeNHX3 from the tree halophyte Populus euphratica in yeast by model-guided mutagenesis.</ArticleTitle><Pagination><MedlinePgn>e104147</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0104147</ELocationID><Abstract><AbstractText>Na+,K+/H+ antiporters are H+-coupled cotransporters that are crucial for cellular homeostasis. Populus euphratica, a well-known tree halophyte, contains six Na+/H+ antiporter genes (PeNHX1-6) that have been shown to function in salt tolerance. However, the catalytic mechanisms governing their ion transport remain largely unknown. Using the crystal structure of the Na+/H+ antiporter from the Escherichia coli (EcNhaA) as a template, we built the three-dimensional structure of PeNHX3 from P. euphratica. The PeNHX3 model displays the typical TM4-TM11 assembly that is critical for ion binding and translocation. The PeNHX3 structure follows the 'positive-inside' rule and exhibits a typical physicochemical property of the transporter proteins. Four conserved residues, including Tyr149, Asn187, Asp188, and Arg356, are indentified in the TM4-TM11 assembly region of PeNHX3. Mutagenesis analysis showed that these reserved residues were essential for the function of PeNHX3: Asn187 and Asp188 (forming a ND motif) controlled ion binding and translocation, and Tyr149 and Arg356 compensated helix dipoles in the TM4-TM11 assembly. PeNHX3 mediated Na+, K+ and Li+ transport in a yeast growth assay. Domain-switch analysis shows that TM11 is crucial to Li+ transport. The novel features of PeNHX3 in ion binding and translocation are discussed. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Liguang</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>MOE Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou, Gansu, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Feng</LastName><ForeName>Xueying</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>MOE Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou, Gansu, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhao</LastName><ForeName>Hong</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>MOE Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou, Gansu, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Lidong</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>MOE Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou, Gansu, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>An</LastName><ForeName>Lizhe</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>MOE Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou, Gansu, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Qiu</LastName><ForeName>Quan-Sheng</ForeName><Initials>QS</Initials><AffiliationInfo><Affiliation>MOE Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou, Gansu, China.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>08</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029968">Escherichia coli Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C102839">NhaA protein, E coli</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017923">Sodium-Hydrogen Exchangers</NameOfSubstance></Chemical><Chemical><RegistryNumber>9FN79X2M3F</RegistryNumber><NameOfSubstance UI="D008094">Lithium</NameOfSubstance></Chemical><Chemical><RegistryNumber>9NEZ333N27</RegistryNumber><NameOfSubstance UI="D012964">Sodium</NameOfSubstance></Chemical><Chemical><RegistryNumber>RWP5GA015D</RegistryNumber><NameOfSubstance UI="D011188">Potassium</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="ErratumIn"><RefSource>PLoS One. 2015;10(2):e0117869</RefSource><PMID Version="1">25646763</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001692" MajorTopicYN="N">Biological 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