Karyopherin-mediated nuclear import of the homing endonuclease VMA1-derived endonuclease is required for self-propagation of the coding region.
Identifieur interne : 001936 ( Main/Exploration ); précédent : 001935; suivant : 001937Karyopherin-mediated nuclear import of the homing endonuclease VMA1-derived endonuclease is required for self-propagation of the coding region.
Auteurs : Yuri Nagai [Japon] ; Satoru Nogami ; Fumi Kumagai-Sano ; Yoshikazu OhyaSource :
- Molecular and cellular biology [ 0270-7306 ] ; 2003.
Descripteurs français
- KwdFr :
- Allèles (MeSH), Azote (métabolisme), Carbone (métabolisme), Cariophérines alpha (métabolisme), Caryophérines (métabolisme), Cytoplasme (métabolisme), Différenciation cellulaire (MeSH), Division cellulaire (MeSH), Endonucleases (métabolisme), Facteurs temps (MeSH), Fermentation (MeSH), Immunotransfert (MeSH), Microscopie de fluorescence (MeSH), Mitose (MeSH), Modèles biologiques (MeSH), Méiose (MeSH), Noyau de la cellule (métabolisme), Plasmides (métabolisme), Proton-Translocating ATPases (métabolisme), Protéines de Saccharomyces cerevisiae (métabolisme), Réaction de polymérisation en chaîne (MeSH), Saccharomyces cerevisiae (métabolisme), Sirolimus (pharmacologie), Structure tertiaire des protéines (MeSH), Techniques de double hybride (MeSH), Transduction du signal (MeSH), Transport nucléaire actif (MeSH).
- MESH :
- métabolisme : Azote, Carbone, Cariophérines alpha, Caryophérines, Cytoplasme, Endonucleases, Noyau de la cellule, Plasmides, Proton-Translocating ATPases, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- pharmacologie : Sirolimus.
- Allèles, Différenciation cellulaire, Division cellulaire, Facteurs temps, Fermentation, Immunotransfert, Microscopie de fluorescence, Mitose, Modèles biologiques, Méiose, Réaction de polymérisation en chaîne, Structure tertiaire des protéines, Techniques de double hybride, Transduction du signal, Transport nucléaire actif.
English descriptors
- KwdEn :
- Active Transport, Cell Nucleus (MeSH), Alleles (MeSH), Carbon (metabolism), Cell Differentiation (MeSH), Cell Division (MeSH), Cell Nucleus (metabolism), Cytoplasm (metabolism), Endonucleases (metabolism), Fermentation (MeSH), Immunoblotting (MeSH), Karyopherins (metabolism), Meiosis (MeSH), Microscopy, Fluorescence (MeSH), Mitosis (MeSH), Models, Biological (MeSH), Nitrogen (metabolism), Plasmids (metabolism), Polymerase Chain Reaction (MeSH), Protein Structure, Tertiary (MeSH), Proton-Translocating ATPases (metabolism), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (MeSH), Sirolimus (pharmacology), Time Factors (MeSH), Two-Hybrid System Techniques (MeSH), alpha Karyopherins (metabolism).
- MESH :
- chemical , metabolism : Carbon, Endonucleases, Karyopherins, Nitrogen, Proton-Translocating ATPases, Saccharomyces cerevisiae Proteins, alpha Karyopherins.
- metabolism : Cell Nucleus, Cytoplasm, Plasmids, Saccharomyces cerevisiae.
- chemical , pharmacology : Sirolimus.
- Active Transport, Cell Nucleus, Alleles, Cell Differentiation, Cell Division, Fermentation, Immunoblotting, Meiosis, Microscopy, Fluorescence, Mitosis, Models, Biological, Polymerase Chain Reaction, Protein Structure, Tertiary, Signal Transduction, Time Factors, Two-Hybrid System Techniques.
Abstract
VMA1-derived endonuclease (VDE), a site-specific endonuclease in Saccharomyces cerevisiae, enters the nucleus to generate a double-strand break in the VDE-negative allelic locus, mediating the self-propagating gene conversion called homing. Although VDE is excluded from the nucleus in mitotic cells, it relocalizes at premeiosis, becoming localized in both the nucleus and the cytoplasm in meiosis. The nuclear localization of VDE is induced by inactivation of TOR kinases, which constitute central regulators of cell differentiation in S. cerevisiae, and by nutrient depletion. A functional genomic approach revealed that at least two karyopherins, Srp1p and Kap142p, are required for the nuclear localization pattern. Genetic and physical interactions between Srp1p and VDE imply direct involvement of karyopherin-mediated nuclear transport in this process. Inactivation of TOR signaling or acquisition of an extra nuclear localization signal in the VDE coding region leads to artificial nuclear localization of VDE and thereby induces homing even during mitosis. These results serve as evidence that VDE utilizes the host systems of nutrient signal transduction and nucleocytoplasmic transport to ensure the propagation of its coding region.
DOI: 10.1128/mcb.23.5.1726-1736.2003
PubMed: 12588991
PubMed Central: PMC151704
Affiliations:
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(metabolism)</term><term>Fermentation (MeSH)</term><term>Immunoblotting (MeSH)</term><term>Karyopherins (metabolism)</term><term>Meiosis (MeSH)</term><term>Microscopy, Fluorescence (MeSH)</term><term>Mitosis (MeSH)</term><term>Models, Biological (MeSH)</term><term>Nitrogen (metabolism)</term><term>Plasmids (metabolism)</term><term>Polymerase Chain Reaction (MeSH)</term><term>Protein Structure, Tertiary (MeSH)</term><term>Proton-Translocating ATPases (metabolism)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Signal Transduction (MeSH)</term><term>Sirolimus (pharmacology)</term><term>Time Factors (MeSH)</term><term>Two-Hybrid System Techniques (MeSH)</term><term>alpha Karyopherins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Allèles (MeSH)</term><term>Azote (métabolisme)</term><term>Carbone (métabolisme)</term><term>Cariophérines alpha (métabolisme)</term><term>Caryophérines (métabolisme)</term><term>Cytoplasme (métabolisme)</term><term>Différenciation cellulaire (MeSH)</term><term>Division cellulaire (MeSH)</term><term>Endonucleases (métabolisme)</term><term>Facteurs temps (MeSH)</term><term>Fermentation (MeSH)</term><term>Immunotransfert (MeSH)</term><term>Microscopie de fluorescence (MeSH)</term><term>Mitose (MeSH)</term><term>Modèles biologiques (MeSH)</term><term>Méiose (MeSH)</term><term>Noyau de la cellule (métabolisme)</term><term>Plasmides (métabolisme)</term><term>Proton-Translocating ATPases (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Réaction de polymérisation en chaîne (MeSH)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Sirolimus (pharmacologie)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Techniques de double hybride (MeSH)</term><term>Transduction du signal (MeSH)</term><term>Transport nucléaire actif (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carbon</term><term>Endonucleases</term><term>Karyopherins</term><term>Nitrogen</term><term>Proton-Translocating ATPases</term><term>Saccharomyces cerevisiae Proteins</term><term>alpha Karyopherins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Nucleus</term><term>Cytoplasm</term><term>Plasmids</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Azote</term><term>Carbone</term><term>Cariophérines alpha</term><term>Caryophérines</term><term>Cytoplasme</term><term>Endonucleases</term><term>Noyau de la cellule</term><term>Plasmides</term><term>Proton-Translocating ATPases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Sirolimus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Sirolimus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Active Transport, Cell Nucleus</term><term>Alleles</term><term>Cell Differentiation</term><term>Cell Division</term><term>Fermentation</term><term>Immunoblotting</term><term>Meiosis</term><term>Microscopy, Fluorescence</term><term>Mitosis</term><term>Models, Biological</term><term>Polymerase Chain Reaction</term><term>Protein Structure, Tertiary</term><term>Signal Transduction</term><term>Time Factors</term><term>Two-Hybrid System Techniques</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Allèles</term><term>Différenciation cellulaire</term><term>Division cellulaire</term><term>Facteurs temps</term><term>Fermentation</term><term>Immunotransfert</term><term>Microscopie de fluorescence</term><term>Mitose</term><term>Modèles biologiques</term><term>Méiose</term><term>Réaction de polymérisation en chaîne</term><term>Structure tertiaire des protéines</term><term>Techniques de double hybride</term><term>Transduction du signal</term><term>Transport nucléaire actif</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">VMA1-derived endonuclease (VDE), a site-specific endonuclease in Saccharomyces cerevisiae, enters the nucleus to generate a double-strand break in the VDE-negative allelic locus, mediating the self-propagating gene conversion called homing. Although VDE is excluded from the nucleus in mitotic cells, it relocalizes at premeiosis, becoming localized in both the nucleus and the cytoplasm in meiosis. The nuclear localization of VDE is induced by inactivation of TOR kinases, which constitute central regulators of cell differentiation in S. cerevisiae, and by nutrient depletion. A functional genomic approach revealed that at least two karyopherins, Srp1p and Kap142p, are required for the nuclear localization pattern. Genetic and physical interactions between Srp1p and VDE imply direct involvement of karyopherin-mediated nuclear transport in this process. Inactivation of TOR signaling or acquisition of an extra nuclear localization signal in the VDE coding region leads to artificial nuclear localization of VDE and thereby induces homing even during mitosis. These results serve as evidence that VDE utilizes the host systems of nutrient signal transduction and nucleocytoplasmic transport to ensure the propagation of its coding region.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12588991</PMID><DateCompleted><Year>2003</Year><Month>04</Month><Day>04</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0270-7306</ISSN><JournalIssue CitedMedium="Print"><Volume>23</Volume><Issue>5</Issue><PubDate><Year>2003</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Molecular and cellular biology</Title><ISOAbbreviation>Mol Cell Biol</ISOAbbreviation></Journal><ArticleTitle>Karyopherin-mediated nuclear import of the homing endonuclease VMA1-derived endonuclease is required for self-propagation of the coding region.</ArticleTitle><Pagination><MedlinePgn>1726-36</MedlinePgn></Pagination><Abstract><AbstractText>VMA1-derived endonuclease (VDE), a site-specific endonuclease in Saccharomyces cerevisiae, enters the nucleus to generate a double-strand break in the VDE-negative allelic locus, mediating the self-propagating gene conversion called homing. Although VDE is excluded from the nucleus in mitotic cells, it relocalizes at premeiosis, becoming localized in both the nucleus and the cytoplasm in meiosis. The nuclear localization of VDE is induced by inactivation of TOR kinases, which constitute central regulators of cell differentiation in S. cerevisiae, and by nutrient depletion. A functional genomic approach revealed that at least two karyopherins, Srp1p and Kap142p, are required for the nuclear localization pattern. Genetic and physical interactions between Srp1p and VDE imply direct involvement of karyopherin-mediated nuclear transport in this process. Inactivation of TOR signaling or acquisition of an extra nuclear localization signal in the VDE coding region leads to artificial nuclear localization of VDE and thereby induces homing even during mitosis. These results serve as evidence that VDE utilizes the host systems of nutrient signal transduction and nucleocytoplasmic transport to ensure the propagation of its coding region.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nagai</LastName><ForeName>Yuri</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Integrated Biosciences, Graduate School of Frontier Sciences, University of Tokyo, Kashiwa, Chiba Prefecture, 277-8562 Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nogami</LastName><ForeName>Satoru</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Kumagai-Sano</LastName><ForeName>Fumi</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Ohya</LastName><ForeName>Yoshikazu</ForeName><Initials>Y</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Mol Cell Biol</MedlineTA><NlmUniqueID>8109087</NlmUniqueID><ISSNLinking>0270-7306</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C423142">KPNA1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D028884">Karyopherins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D028901">alpha Karyopherins</NameOfSubstance></Chemical><Chemical><RegistryNumber>7440-44-0</RegistryNumber><NameOfSubstance UI="D002244">Carbon</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.-</RegistryNumber><NameOfSubstance UI="D004720">Endonucleases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.3.14</RegistryNumber><NameOfSubstance UI="D006180">Proton-Translocating ATPases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 7.1.2.2</RegistryNumber><NameOfSubstance UI="C081687">VMA1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>N762921K75</RegistryNumber><NameOfSubstance UI="D009584">Nitrogen</NameOfSubstance></Chemical><Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D021581" MajorTopicYN="N">Active Transport, Cell Nucleus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000483" MajorTopicYN="N">Alleles</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002244" MajorTopicYN="N">Carbon</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002454" MajorTopicYN="N">Cell Differentiation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002455" MajorTopicYN="N">Cell Division</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002467" MajorTopicYN="N">Cell Nucleus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003593" MajorTopicYN="N">Cytoplasm</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004720" MajorTopicYN="N">Endonucleases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005285" MajorTopicYN="N">Fermentation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015151" MajorTopicYN="N">Immunoblotting</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D028884" MajorTopicYN="N">Karyopherins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008540" MajorTopicYN="N">Meiosis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008856" MajorTopicYN="N">Microscopy, Fluorescence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008938" MajorTopicYN="N">Mitosis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008954" MajorTopicYN="N">Models, Biological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009584" MajorTopicYN="N">Nitrogen</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010957" MajorTopicYN="N">Plasmids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016133" MajorTopicYN="N">Polymerase Chain Reaction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006180" MajorTopicYN="N">Proton-Translocating ATPases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020123" MajorTopicYN="N">Sirolimus</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013997" MajorTopicYN="N">Time Factors</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020798" MajorTopicYN="N">Two-Hybrid System Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D028901" MajorTopicYN="N">alpha Karyopherins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2003</Year><Month>2</Month><Day>18</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2003</Year><Month>4</Month><Day>5</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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Kantō</li></region><settlement><li>Tokyo</li></settlement><orgName><li>Université de Tokyo</li></orgName></list><tree><noCountry><name sortKey="Kumagai Sano, Fumi" sort="Kumagai Sano, Fumi" uniqKey="Kumagai Sano F" first="Fumi" last="Kumagai-Sano">Fumi Kumagai-Sano</name><name sortKey="Nogami, Satoru" sort="Nogami, Satoru" uniqKey="Nogami S" first="Satoru" last="Nogami">Satoru Nogami</name><name sortKey="Ohya, Yoshikazu" sort="Ohya, Yoshikazu" uniqKey="Ohya Y" first="Yoshikazu" last="Ohya">Yoshikazu Ohya</name></noCountry><country name="Japon"><region name="Région de Kantō"><name sortKey="Nagai, Yuri" sort="Nagai, Yuri" uniqKey="Nagai Y" first="Yuri" last="Nagai">Yuri Nagai</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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