The ribosomal DNA metaphase loop of Saccharomyces cerevisiae gets condensed upon heat stress in a Cdc14-independent TORC1-dependent manner.
Identifieur interne : 000447 ( Main/Exploration ); précédent : 000446; suivant : 000448The ribosomal DNA metaphase loop of Saccharomyces cerevisiae gets condensed upon heat stress in a Cdc14-independent TORC1-dependent manner.
Auteurs : Emiliano Matos-Perdomo [Espagne] ; Félix Machín [Espagne]Source :
- Cell cycle (Georgetown, Tex.) [ 1551-4005 ] ; 2018.
Descripteurs français
- KwdFr :
- ADN ribosomique (composition chimique), Acides indolacétiques (MeSH), Adenosine triphosphatases (métabolisme), Anaphase (MeSH), Complexes multiprotéiques (métabolisme), Facteurs de transcription (antagonistes et inhibiteurs), Facteurs de transcription (physiologie), Métaphase (génétique), Protein Tyrosine Phosphatases (métabolisme), Protein-Serine-Threonine Kinases (métabolisme), Protéines G (métabolisme), Protéines de Saccharomyces cerevisiae (antagonistes et inhibiteurs), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines de Saccharomyces cerevisiae (physiologie), Protéines de liaison à l'ADN (métabolisme), Protéines du cycle cellulaire (métabolisme), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Température élevée (MeSH), Télophase (MeSH).
- MESH :
- antagonistes et inhibiteurs : Facteurs de transcription, Protéines de Saccharomyces cerevisiae.
- composition chimique : ADN ribosomique.
- génétique : Métaphase, Saccharomyces cerevisiae.
- métabolisme : Adenosine triphosphatases, Complexes multiprotéiques, Protein Tyrosine Phosphatases, Protein-Serine-Threonine Kinases, Protéines G, Protéines de Saccharomyces cerevisiae, Protéines de liaison à l'ADN, Protéines du cycle cellulaire, Saccharomyces cerevisiae.
- physiologie : Facteurs de transcription, Protéines de Saccharomyces cerevisiae.
- Acides indolacétiques, Anaphase, Température élevée, Télophase.
English descriptors
- KwdEn :
- Adenosine Triphosphatases (metabolism), Anaphase (MeSH), Cell Cycle Proteins (metabolism), DNA, Ribosomal (chemistry), DNA-Binding Proteins (metabolism), GTP-Binding Proteins (metabolism), Hot Temperature (MeSH), Indoleacetic Acids (MeSH), Metaphase (genetics), Multiprotein Complexes (metabolism), Protein Tyrosine Phosphatases (metabolism), Protein-Serine-Threonine Kinases (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (antagonists & inhibitors), Saccharomyces cerevisiae Proteins (metabolism), Saccharomyces cerevisiae Proteins (physiology), Telophase (MeSH), Transcription Factors (antagonists & inhibitors), Transcription Factors (physiology).
- MESH :
- chemical , antagonists & inhibitors : Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , chemistry : DNA, Ribosomal.
- chemical , metabolism : Adenosine Triphosphatases, Cell Cycle Proteins, DNA-Binding Proteins, GTP-Binding Proteins, Multiprotein Complexes, Protein Tyrosine Phosphatases, Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins.
- genetics : Metaphase, Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- chemical , physiology : Saccharomyces cerevisiae Proteins, Transcription Factors.
- Anaphase, Hot Temperature, Indoleacetic Acids, Telophase.
Abstract
Chromosome morphology in Saccharomyces cerevisiae is only visible at the microscopic level in the ribosomal DNA array (rDNA). The rDNA has been thus used as a model to characterize condensation and segregation of sister chromatids in mitosis. It has been established that the metaphase structure ("loop") depends, among others, on the condensin complex; whereas its segregation also depends on that complex, the Polo-like kinase Cdc5 and the cell cycle master phosphatase Cdc14. In addition, Cdc14 also drives rDNA hypercondensation in telophase. Remarkably, since all these components are essential for cell survival, their role on rDNA condensation and segregation was established by temperature-sensitive (ts) alleles. Here, we show that the heat stress (HS) used to inactivate ts alleles (25 ºC to 37 ºC shift) causes rDNA loop condensation in metaphase-arrested wild type cells, a result that can also be mimicked by other stresses that inhibit the TORC1 pathway. Because this condensation might challenge previous findings with ts alleles, we have repeated classical experiments of rDNA condensation and segregation, yet using instead auxin-driven degradation alleles (aid alleles). We have undertaken the protein degradation at lower temperatures (25 ºC) and concluded that the classical roles for condensin, Cdc5, Cdc14 and Cdc15 still prevailed. Thus, condensin degradation disrupts rDNA higher organization, Cdc14 and Cdc5 degradation precludes rDNA segregation and Cdc15 degradation still allows rDNA hypercompaction in telophase. Finally, we provide direct genetic evidence that this HS-mediated rDNA condensation is dependent on TORC1 but, unlike the one observed in anaphase, is independent of Cdc14.
DOI: 10.1080/15384101.2017.1407890
PubMed: 29166821
PubMed Central: PMC5884360
Affiliations:
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Le document en format XML
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élevée</term><term>Télophase</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Chromosome morphology in Saccharomyces cerevisiae is only visible at the microscopic level in the ribosomal DNA array (rDNA). The rDNA has been thus used as a model to characterize condensation and segregation of sister chromatids in mitosis. It has been established that the metaphase structure ("loop") depends, among others, on the condensin complex; whereas its segregation also depends on that complex, the Polo-like kinase Cdc5 and the cell cycle master phosphatase Cdc14. In addition, Cdc14 also drives rDNA hypercondensation in telophase. Remarkably, since all these components are essential for cell survival, their role on rDNA condensation and segregation was established by temperature-sensitive (ts) alleles. Here, we show that the heat stress (HS) used to inactivate ts alleles (25 ºC to 37 ºC shift) causes rDNA loop condensation in metaphase-arrested wild type cells, a result that can also be mimicked by other stresses that inhibit the TORC1 pathway. Because this condensation might challenge previous findings with ts alleles, we have repeated classical experiments of rDNA condensation and segregation, yet using instead auxin-driven degradation alleles (aid alleles). We have undertaken the protein degradation at lower temperatures (25 ºC) and concluded that the classical roles for condensin, Cdc5, Cdc14 and Cdc15 still prevailed. Thus, condensin degradation disrupts rDNA higher organization, Cdc14 and Cdc5 degradation precludes rDNA segregation and Cdc15 degradation still allows rDNA hypercompaction in telophase. Finally, we provide direct genetic evidence that this HS-mediated rDNA condensation is dependent on TORC1 but, unlike the one observed in anaphase, is independent of Cdc14.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29166821</PMID><DateCompleted><Year>2019</Year><Month>08</Month><Day>29</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1551-4005</ISSN><JournalIssue CitedMedium="Internet"><Volume>17</Volume><Issue>2</Issue><PubDate><Year>2018</Year></PubDate></JournalIssue><Title>Cell cycle (Georgetown, Tex.)</Title><ISOAbbreviation>Cell Cycle</ISOAbbreviation></Journal><ArticleTitle>The ribosomal DNA metaphase loop of Saccharomyces cerevisiae gets condensed upon heat stress in a Cdc14-independent TORC1-dependent manner.</ArticleTitle><Pagination><MedlinePgn>200-215</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1080/15384101.2017.1407890</ELocationID><Abstract><AbstractText>Chromosome morphology in Saccharomyces cerevisiae is only visible at the microscopic level in the ribosomal DNA array (rDNA). The rDNA has been thus used as a model to characterize condensation and segregation of sister chromatids in mitosis. It has been established that the metaphase structure ("loop") depends, among others, on the condensin complex; whereas its segregation also depends on that complex, the Polo-like kinase Cdc5 and the cell cycle master phosphatase Cdc14. In addition, Cdc14 also drives rDNA hypercondensation in telophase. Remarkably, since all these components are essential for cell survival, their role on rDNA condensation and segregation was established by temperature-sensitive (ts) alleles. Here, we show that the heat stress (HS) used to inactivate ts alleles (25 ºC to 37 ºC shift) causes rDNA loop condensation in metaphase-arrested wild type cells, a result that can also be mimicked by other stresses that inhibit the TORC1 pathway. Because this condensation might challenge previous findings with ts alleles, we have repeated classical experiments of rDNA condensation and segregation, yet using instead auxin-driven degradation alleles (aid alleles). We have undertaken the protein degradation at lower temperatures (25 ºC) and concluded that the classical roles for condensin, Cdc5, Cdc14 and Cdc15 still prevailed. Thus, condensin degradation disrupts rDNA higher organization, Cdc14 and Cdc5 degradation precludes rDNA segregation and Cdc15 degradation still allows rDNA hypercompaction in telophase. Finally, we provide direct genetic evidence that this HS-mediated rDNA condensation is dependent on TORC1 but, unlike the one observed in anaphase, is independent of Cdc14.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Matos-Perdomo</LastName><ForeName>Emiliano</ForeName><Initials>E</Initials><Identifier Source="ORCID">0000-0001-9783-3591</Identifier><AffiliationInfo><Affiliation>a Unidad de Investigación , Hospital Universitario Ntra Sra de Candelaria , Ctra del Rosario 145, 38010 , Santa Cruz de Tenerife , Spain.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>b Universidad de La Laguna , Tenerife , Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Machín</LastName><ForeName>Félix</ForeName><Initials>F</Initials><Identifier Source="ORCID">0000-0003-4559-7798</Identifier><AffiliationInfo><Affiliation>a Unidad de Investigación , Hospital Universitario Ntra Sra de Candelaria , Ctra del Rosario 145, 38010 , Santa Cruz de Tenerife , Spain.</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>2018</Year><Month>01</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Cell Cycle</MedlineTA><NlmUniqueID>101137841</NlmUniqueID><ISSNLinking>1551-4005</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C074860">CDC14 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C082279">CDC15 protein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018797">Cell Cycle Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004275">DNA, Ribosomal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004268">DNA-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007210">Indoleacetic Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D046912">Multiprotein Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C561842">TORC1 protein complex, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C108312">condensin complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.21</RegistryNumber><NameOfSubstance UI="C081927">CDC5 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.3.48</RegistryNumber><NameOfSubstance UI="D017027">Protein Tyrosine Phosphatases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber><NameOfSubstance UI="D000251">Adenosine Triphosphatases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber><NameOfSubstance UI="D019204">GTP-Binding Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000251" MajorTopicYN="N">Adenosine Triphosphatases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000705" MajorTopicYN="N">Anaphase</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018797" MajorTopicYN="N">Cell Cycle Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004275" MajorTopicYN="N">DNA, Ribosomal</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004268" MajorTopicYN="N">DNA-Binding Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019204" MajorTopicYN="N">GTP-Binding Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006358" MajorTopicYN="Y">Hot Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007210" MajorTopicYN="N">Indoleacetic Acids</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008677" MajorTopicYN="N">Metaphase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D046912" MajorTopicYN="N">Multiprotein Complexes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017027" MajorTopicYN="N">Protein Tyrosine Phosphatases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013692" MajorTopicYN="N">Telophase</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Cdc14</Keyword><Keyword MajorTopicYN="Y">Cdc15</Keyword><Keyword MajorTopicYN="Y">Cdc5</Keyword><Keyword MajorTopicYN="Y">Cdc60</Keyword><Keyword MajorTopicYN="Y">Heat stress</Keyword><Keyword MajorTopicYN="Y">TORC1</Keyword><Keyword MajorTopicYN="Y">aid degron</Keyword><Keyword MajorTopicYN="Y">condensin</Keyword><Keyword MajorTopicYN="Y">rapamycin</Keyword><Keyword MajorTopicYN="Y">ribosomal DNA</Keyword><Keyword MajorTopicYN="Y">temperature-sensitive allele</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>11</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>8</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>11</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29166821</ArticleId><ArticleId 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