The putative transcription factor CaMaf1 controls the sensitivity to lithium and rapamycin and represses RNA polymerase III transcription in Candida albicans.
Identifieur interne : 000448 ( Main/Exploration ); précédent : 000447; suivant : 000449The putative transcription factor CaMaf1 controls the sensitivity to lithium and rapamycin and represses RNA polymerase III transcription in Candida albicans.
Auteurs : Faiza Asghar [République populaire de Chine] ; Hongbo Yan [République populaire de Chine] ; Linghuo Jiang [République populaire de Chine]Source :
- FEMS yeast research [ 1567-1364 ] ; 2018.
Descripteurs français
- KwdFr :
- ARN de transfert (métabolisme), Antifongiques (pharmacologie), Candida albicans (cytologie), Candida albicans (effets des médicaments et des substances chimiques), Candida albicans (génétique), Candida albicans (métabolisme), Cytoplasme (métabolisme), Délétion de gène (MeSH), Facteurs de transcription (composition chimique), Facteurs de transcription (génétique), Facteurs de transcription (métabolisme), Geranyltranstransferase (génétique), Noyau de la cellule (métabolisme), Protéines de répression (composition chimique), Protéines de répression (génétique), Protéines de répression (métabolisme), Protéines fongiques (composition chimique), Protéines fongiques (génétique), Protéines fongiques (métabolisme), RNA polymerase III (génétique), Régulation de l'expression des gènes fongiques (MeSH), Séquence d'acides aminés (MeSH), Tests de sensibilité microbienne (MeSH), Tolérance aux médicaments (génétique), Transcription génétique (MeSH).
- MESH :
- composition chimique : Facteurs de transcription, Protéines de répression, Protéines fongiques.
- cytologie : Candida albicans.
- effets des médicaments et des substances chimiques : Candida albicans.
- génétique : Candida albicans, Facteurs de transcription, Geranyltranstransferase, Protéines de répression, Protéines fongiques, RNA polymerase III, Tolérance aux médicaments.
- métabolisme : ARN de transfert, Candida albicans, Cytoplasme, Facteurs de transcription, Noyau de la cellule, Protéines de répression, Protéines fongiques.
- pharmacologie : Antifongiques.
- Délétion de gène, Régulation de l'expression des gènes fongiques, Séquence d'acides aminés, Tests de sensibilité microbienne, Transcription génétique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Antifungal Agents (pharmacology), Candida albicans (cytology), Candida albicans (drug effects), Candida albicans (genetics), Candida albicans (metabolism), Cell Nucleus (metabolism), Cytoplasm (metabolism), Drug Tolerance (genetics), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Gene Deletion (MeSH), Gene Expression Regulation, Fungal (MeSH), Geranyltranstransferase (genetics), Microbial Sensitivity Tests (MeSH), RNA Polymerase III (genetics), RNA, Transfer (metabolism), Repressor Proteins (chemistry), Repressor Proteins (genetics), Repressor Proteins (metabolism), Transcription Factors (chemistry), Transcription Factors (genetics), Transcription Factors (metabolism), Transcription, Genetic (MeSH).
- MESH :
- chemical , chemistry : Fungal Proteins, Repressor Proteins, Transcription Factors.
- chemical , genetics : Fungal Proteins, Geranyltranstransferase, RNA Polymerase III, Repressor Proteins, Transcription Factors.
- chemical , metabolism : Fungal Proteins, RNA, Transfer, Repressor Proteins, Transcription Factors.
- chemical , pharmacology : Antifungal Agents.
- cytology : Candida albicans.
- drug effects : Candida albicans.
- genetics : Candida albicans, Drug Tolerance.
- metabolism : Candida albicans, Cell Nucleus, Cytoplasm.
- Amino Acid Sequence, Gene Deletion, Gene Expression Regulation, Fungal, Microbial Sensitivity Tests, Transcription, Genetic.
Abstract
Maf1 is a repressor of RNA polymerase (Pol) III transcription for tRNA. Nutrient deprivation and environmental stress repress Pol III transcription through Maf1 in Saccharomyces cerevisiae. The sole Candida albicans homolog CaMaf1 is a protein of 380 amino acids with conserved domains and motifs of the eukaryotic Maf1 family. Here, we show that C. albicans cells lacking CaMAF1 show elevated levels of tRNA. Deletion of CaMAF1 increases the sensitivity of C. albicans cells to lithium cation and SDS as well as tolerance to rapamycin and azole. In addition, deletion of CaMAF1 reduces the level of filamentation and alters the surface morphology of colonies. CaMaf1 is localized in the nucleus of log-phase growing cells. However, a dynamic change of subcellular localization of CaMaf1 exists during serum-induced morphological transition, with CaMaf1 being localized in the nuclei of cells with germ tubes and short filaments but outside of the nuclei of cells with long filaments. In addition, CaMaf1 is required for rapamycin-induced repression of CaERG20, encoding the farnesyl pyrophosphate synthetase involved in ergosterol biosynthesis. Therefore, CaMaf1 plays a role as a general repressor of Pol III transcription in C. albicans.
DOI: 10.1093/femsyr/foy068
PubMed: 29982370
Affiliations:
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(metabolism)</term><term>Transcription Factors (chemistry)</term><term>Transcription Factors (genetics)</term><term>Transcription Factors (metabolism)</term><term>Transcription, Genetic (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN de transfert (métabolisme)</term><term>Antifongiques (pharmacologie)</term><term>Candida albicans (cytologie)</term><term>Candida albicans (effets des médicaments et des substances chimiques)</term><term>Candida albicans (génétique)</term><term>Candida albicans (métabolisme)</term><term>Cytoplasme (métabolisme)</term><term>Délétion de gène (MeSH)</term><term>Facteurs de transcription (composition chimique)</term><term>Facteurs de transcription (génétique)</term><term>Facteurs de transcription (métabolisme)</term><term>Geranyltranstransferase (génétique)</term><term>Noyau de la cellule (métabolisme)</term><term>Protéines de répression (composition chimique)</term><term>Protéines de répression (génétique)</term><term>Protéines de répression (métabolisme)</term><term>Protéines fongiques (composition chimique)</term><term>Protéines fongiques (génétique)</term><term>Protéines fongiques (métabolisme)</term><term>RNA polymerase III (génétique)</term><term>Régulation de l'expression des gènes fongiques (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Tests de sensibilité microbienne (MeSH)</term><term>Tolérance aux médicaments (génétique)</term><term>Transcription génétique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Fungal Proteins</term><term>Repressor Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fungal Proteins</term><term>Geranyltranstransferase</term><term>RNA Polymerase III</term><term>Repressor Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fungal Proteins</term><term>RNA, Transfer</term><term>Repressor Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antifungal Agents</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Facteurs de transcription</term><term>Protéines de répression</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Candida albicans</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Candida albicans</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Candida albicans</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Candida albicans</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Candida albicans</term><term>Drug Tolerance</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Candida albicans</term><term>Facteurs de transcription</term><term>Geranyltranstransferase</term><term>Protéines de répression</term><term>Protéines fongiques</term><term>RNA polymerase III</term><term>Tolérance aux médicaments</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Candida albicans</term><term>Cell Nucleus</term><term>Cytoplasm</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN de transfert</term><term>Candida albicans</term><term>Cytoplasme</term><term>Facteurs de transcription</term><term>Noyau de la cellule</term><term>Protéines de répression</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antifongiques</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Gene Deletion</term><term>Gene Expression Regulation, Fungal</term><term>Microbial Sensitivity Tests</term><term>Transcription, Genetic</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Délétion de gène</term><term>Régulation de l'expression des gènes fongiques</term><term>Séquence d'acides aminés</term><term>Tests de sensibilité microbienne</term><term>Transcription génétique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Maf1 is a repressor of RNA polymerase (Pol) III transcription for tRNA. Nutrient deprivation and environmental stress repress Pol III transcription through Maf1 in Saccharomyces cerevisiae. The sole Candida albicans homolog CaMaf1 is a protein of 380 amino acids with conserved domains and motifs of the eukaryotic Maf1 family. Here, we show that C. albicans cells lacking CaMAF1 show elevated levels of tRNA. Deletion of CaMAF1 increases the sensitivity of C. albicans cells to lithium cation and SDS as well as tolerance to rapamycin and azole. In addition, deletion of CaMAF1 reduces the level of filamentation and alters the surface morphology of colonies. CaMaf1 is localized in the nucleus of log-phase growing cells. However, a dynamic change of subcellular localization of CaMaf1 exists during serum-induced morphological transition, with CaMaf1 being localized in the nuclei of cells with germ tubes and short filaments but outside of the nuclei of cells with long filaments. In addition, CaMaf1 is required for rapamycin-induced repression of CaERG20, encoding the farnesyl pyrophosphate synthetase involved in ergosterol biosynthesis. Therefore, CaMaf1 plays a role as a general repressor of Pol III transcription in C. albicans.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29982370</PMID><DateCompleted><Year>2019</Year><Month>05</Month><Day>16</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>16</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1567-1364</ISSN><JournalIssue CitedMedium="Internet"><Volume>18</Volume><Issue>6</Issue><PubDate><Year>2018</Year><Month>09</Month><Day>01</Day></PubDate></JournalIssue><Title>FEMS yeast research</Title><ISOAbbreviation>FEMS Yeast Res</ISOAbbreviation></Journal><ArticleTitle>The putative transcription factor CaMaf1 controls the sensitivity to lithium and rapamycin and represses RNA polymerase III transcription in Candida albicans.</ArticleTitle><ELocationID EIdType="doi" ValidYN="Y">10.1093/femsyr/foy068</ELocationID><Abstract><AbstractText>Maf1 is a repressor of RNA polymerase (Pol) III transcription for tRNA. Nutrient deprivation and environmental stress repress Pol III transcription through Maf1 in Saccharomyces cerevisiae. The sole Candida albicans homolog CaMaf1 is a protein of 380 amino acids with conserved domains and motifs of the eukaryotic Maf1 family. Here, we show that C. albicans cells lacking CaMAF1 show elevated levels of tRNA. Deletion of CaMAF1 increases the sensitivity of C. albicans cells to lithium cation and SDS as well as tolerance to rapamycin and azole. In addition, deletion of CaMAF1 reduces the level of filamentation and alters the surface morphology of colonies. CaMaf1 is localized in the nucleus of log-phase growing cells. However, a dynamic change of subcellular localization of CaMaf1 exists during serum-induced morphological transition, with CaMaf1 being localized in the nuclei of cells with germ tubes and short filaments but outside of the nuclei of cells with long filaments. In addition, CaMaf1 is required for rapamycin-induced repression of CaERG20, encoding the farnesyl pyrophosphate synthetase involved in ergosterol biosynthesis. Therefore, CaMaf1 plays a role as a general repressor of Pol III transcription in C. albicans.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Asghar</LastName><ForeName>Faiza</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Laboratory for Yeast Molecular and Cell Biology, the Research Center of Fermentation Technology, School of Agricultural Engineering and Food Science, Shandong University of Technology, 266 XiCunXi Road, Zibo 255000, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yan</LastName><ForeName>Hongbo</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Laboratory for Yeast Molecular and Cell Biology, the Research Center of Fermentation Technology, School of Agricultural Engineering and Food Science, Shandong University of Technology, 266 XiCunXi Road, Zibo 255000, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jiang</LastName><ForeName>Linghuo</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Laboratory for Yeast Molecular and Cell Biology, the Research Center of Fermentation Technology, School of Agricultural Engineering and Food Science, Shandong University of Technology, 266 XiCunXi Road, Zibo 255000, 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></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEMS Yeast Res</MedlineTA><NlmUniqueID>101085384</NlmUniqueID><ISSNLinking>1567-1356</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000935">Antifungal Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012097">Repressor Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>9014-25-9</RegistryNumber><NameOfSubstance UI="D012343">RNA, Transfer</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.1.10</RegistryNumber><NameOfSubstance UI="D051228">Geranyltranstransferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.7.6</RegistryNumber><NameOfSubstance UI="D012320">RNA Polymerase III</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000935" MajorTopicYN="N">Antifungal Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002176" MajorTopicYN="N">Candida albicans</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002467" MajorTopicYN="N">Cell Nucleus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003593" MajorTopicYN="N">Cytoplasm</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004361" MajorTopicYN="N">Drug Tolerance</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017353" MajorTopicYN="N">Gene Deletion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051228" MajorTopicYN="N">Geranyltranstransferase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008826" MajorTopicYN="N">Microbial Sensitivity Tests</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012320" MajorTopicYN="N">RNA Polymerase III</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012343" MajorTopicYN="N">RNA, Transfer</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012097" MajorTopicYN="N">Repressor Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014158" MajorTopicYN="Y">Transcription, Genetic</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>05</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>06</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>7</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>5</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>7</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29982370</ArticleId><ArticleId IdType="pii">5047891</ArticleId><ArticleId IdType="doi">10.1093/femsyr/foy068</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Asghar, Faiza" sort="Asghar, Faiza" uniqKey="Asghar F" first="Faiza" last="Asghar">Faiza Asghar</name></noRegion><name sortKey="Jiang, Linghuo" sort="Jiang, Linghuo" uniqKey="Jiang L" first="Linghuo" last="Jiang">Linghuo Jiang</name><name sortKey="Yan, Hongbo" sort="Yan, Hongbo" uniqKey="Yan H" first="Hongbo" last="Yan">Hongbo Yan</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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