Autoregulation in the biosynthesis of ribosomes.
Identifieur interne : 002475 ( PubMed/Corpus ); précédent : 002474; suivant : 002476Autoregulation in the biosynthesis of ribosomes.
Auteurs : Yu Zhao ; Jung-Hoon Sohn ; Jonathan R. WarnerSource :
- Molecular and cellular biology [ 0270-7306 ] ; 2003.
English descriptors
- KwdEn :
- Blotting, Northern, Cytoplasm (metabolism), DNA Primers (metabolism), Gene Deletion, Gene Expression Regulation, Fungal, Models, Genetic, Mutation, Phenotype, Plasmids (metabolism), Protein Binding, Protein Biosynthesis, RNA (metabolism), RNA, Messenger (metabolism), RNA, Ribosomal (metabolism), Ribosomal Proteins (metabolism), Ribosomes (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Temperature, Time Factors, Transcription, Genetic, Tunicamycin (pharmacology).
- MESH :
- chemical , metabolism : DNA Primers, RNA, RNA, Messenger, RNA, Ribosomal, Ribosomal Proteins.
- genetics : Saccharomyces cerevisiae.
- metabolism : Cytoplasm, Plasmids, Ribosomes, Saccharomyces cerevisiae.
- chemical , pharmacology : Tunicamycin.
- Blotting, Northern, Gene Deletion, Gene Expression Regulation, Fungal, Models, Genetic, Mutation, Phenotype, Protein Binding, Protein Biosynthesis, Temperature, Time Factors, Transcription, Genetic.
Abstract
The synthesis of ribosomes in Saccharomyces cerevisiae consumes a prodigious amount of the cell's resources and, consequently, is tightly regulated. The rate of ribosome synthesis responds not only to nutritional cues but also to signals dependent on other macromolecular pathways of the cell, e.g., a defect in the secretory pathway leads to severe repression of transcription of both rRNA and ribosomal protein genes. A search for mutants that interrupted this repression revealed, surprisingly, that inactivation of RPL1B, one of a pair of genes encoding the 60S ribosomal protein L1, almost completely blocked the repression of rRNA and ribosomal protein gene transcription that usually follows a defect in the secretory pathway. Further experiments showed that almost any mutation leading to a defect in 60S subunit synthesis had the same effect, whereas mutations affecting 40S subunit synthesis did not. Although one might suspect that this effect would be due to a decrease in the initiation of translation or to the presence of half-mers, i.e., polyribosomes awaiting a 60S subunit, our data show that this is not the case. Rather, a variety of experiments suggest that some aspect of the production of defective 60S particles or, more likely, their breakdown suppresses the signal generated by a defect in the secretory pathway that represses ribosome synthesis.
DOI: 10.1128/mcb.23.2.699-707.2003
PubMed: 12509467
Links to Exploration step
pubmed:12509467Le document en format XML
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Warner</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2003">2003</date><idno type="RBID">pubmed:12509467</idno><idno type="pmid">12509467</idno><idno type="doi">10.1128/mcb.23.2.699-707.2003</idno><idno type="wicri:Area/PubMed/Corpus">002475</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002475</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Autoregulation in the biosynthesis of ribosomes.</title><author><name sortKey="Zhao, Yu" sort="Zhao, Yu" uniqKey="Zhao Y" first="Yu" last="Zhao">Yu Zhao</name><affiliation><nlm:affiliation>Department of Cell Biology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Sohn, Jung Hoon" sort="Sohn, Jung Hoon" uniqKey="Sohn J" first="Jung-Hoon" last="Sohn">Jung-Hoon Sohn</name></author><author><name sortKey="Warner, Jonathan R" sort="Warner, Jonathan R" uniqKey="Warner J" first="Jonathan R" last="Warner">Jonathan R. Warner</name></author></analytic><series><title level="j">Molecular and cellular biology</title><idno type="ISSN">0270-7306</idno><imprint><date when="2003" type="published">2003</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Blotting, Northern</term><term>Cytoplasm (metabolism)</term><term>DNA Primers (metabolism)</term><term>Gene Deletion</term><term>Gene Expression Regulation, Fungal</term><term>Models, Genetic</term><term>Mutation</term><term>Phenotype</term><term>Plasmids (metabolism)</term><term>Protein Binding</term><term>Protein Biosynthesis</term><term>RNA (metabolism)</term><term>RNA, Messenger (metabolism)</term><term>RNA, Ribosomal (metabolism)</term><term>Ribosomal Proteins (metabolism)</term><term>Ribosomes (metabolism)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Temperature</term><term>Time Factors</term><term>Transcription, Genetic</term><term>Tunicamycin (pharmacology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA Primers</term><term>RNA</term><term>RNA, Messenger</term><term>RNA, Ribosomal</term><term>Ribosomal Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cytoplasm</term><term>Plasmids</term><term>Ribosomes</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Tunicamycin</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Blotting, Northern</term><term>Gene Deletion</term><term>Gene Expression Regulation, Fungal</term><term>Models, Genetic</term><term>Mutation</term><term>Phenotype</term><term>Protein Binding</term><term>Protein Biosynthesis</term><term>Temperature</term><term>Time Factors</term><term>Transcription, Genetic</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The synthesis of ribosomes in Saccharomyces cerevisiae consumes a prodigious amount of the cell's resources and, consequently, is tightly regulated. The rate of ribosome synthesis responds not only to nutritional cues but also to signals dependent on other macromolecular pathways of the cell, e.g., a defect in the secretory pathway leads to severe repression of transcription of both rRNA and ribosomal protein genes. A search for mutants that interrupted this repression revealed, surprisingly, that inactivation of RPL1B, one of a pair of genes encoding the 60S ribosomal protein L1, almost completely blocked the repression of rRNA and ribosomal protein gene transcription that usually follows a defect in the secretory pathway. Further experiments showed that almost any mutation leading to a defect in 60S subunit synthesis had the same effect, whereas mutations affecting 40S subunit synthesis did not. Although one might suspect that this effect would be due to a decrease in the initiation of translation or to the presence of half-mers, i.e., polyribosomes awaiting a 60S subunit, our data show that this is not the case. Rather, a variety of experiments suggest that some aspect of the production of defective 60S particles or, more likely, their breakdown suppresses the signal generated by a defect in the secretory pathway that represses ribosome synthesis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12509467</PMID><DateCompleted><Year>2003</Year><Month>02</Month><Day>24</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>2</Issue><PubDate><Year>2003</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Molecular and cellular biology</Title><ISOAbbreviation>Mol. Cell. Biol.</ISOAbbreviation></Journal><ArticleTitle>Autoregulation in the biosynthesis of ribosomes.</ArticleTitle><Pagination><MedlinePgn>699-707</MedlinePgn></Pagination><Abstract><AbstractText>The synthesis of ribosomes in Saccharomyces cerevisiae consumes a prodigious amount of the cell's resources and, consequently, is tightly regulated. The rate of ribosome synthesis responds not only to nutritional cues but also to signals dependent on other macromolecular pathways of the cell, e.g., a defect in the secretory pathway leads to severe repression of transcription of both rRNA and ribosomal protein genes. A search for mutants that interrupted this repression revealed, surprisingly, that inactivation of RPL1B, one of a pair of genes encoding the 60S ribosomal protein L1, almost completely blocked the repression of rRNA and ribosomal protein gene transcription that usually follows a defect in the secretory pathway. Further experiments showed that almost any mutation leading to a defect in 60S subunit synthesis had the same effect, whereas mutations affecting 40S subunit synthesis did not. Although one might suspect that this effect would be due to a decrease in the initiation of translation or to the presence of half-mers, i.e., polyribosomes awaiting a 60S subunit, our data show that this is not the case. Rather, a variety of experiments suggest that some aspect of the production of defective 60S particles or, more likely, their breakdown suppresses the signal generated by a defect in the secretory pathway that represses ribosome synthesis.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhao</LastName><ForeName>Yu</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Cell Biology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sohn</LastName><ForeName>Jung-Hoon</ForeName><Initials>JH</Initials></Author><Author ValidYN="Y"><LastName>Warner</LastName><ForeName>Jonathan R</ForeName><Initials>JR</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>P30 CA013330</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM025532</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>CA13330</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM25532</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</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="D017931">DNA 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