Nucleotide degradation and ribose salvage in yeast.
Identifieur interne : 001009 ( Main/Exploration ); précédent : 001008; suivant : 001010Nucleotide degradation and ribose salvage in yeast.
Auteurs : Yi-Fan Xu [États-Unis] ; Fabien Létisse ; Farnaz Absalan ; Wenyun Lu ; Ekaterina Kuznetsova ; Greg Brown ; Amy A. Caudy ; Alexander F. Yakunin ; James R. Broach ; Joshua D. RabinowitzSource :
- Molecular systems biology [ 1744-4292 ] ; 2013.
Descripteurs français
- KwdFr :
- AMP-Activated Protein Kinases (génétique), AMP-Activated Protein Kinases (métabolisme), Cyclic AMP-Dependent Protein Kinases (génétique), Cyclic AMP-Dependent Protein Kinases (métabolisme), Glycéraldéhyde 3-phosphate (métabolisme), N-Glycosyl hydrolases (déficit), N-Glycosyl hydrolases (génétique), NADP (métabolisme), Nucléotides (métabolisme), Oses phosphates (MeSH), Protein-Serine-Threonine Kinases (génétique), Protein-Serine-Threonine Kinases (métabolisme), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Purine nucleoside phosphorylase (déficit), Purine nucleoside phosphorylase (génétique), Ribose (métabolisme), Régulation de l'expression des gènes fongiques (MeSH), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Stress physiologique (génétique), Transaldolase (génétique), Transaldolase (métabolisme), Transduction du signal (MeSH), Voie des pentoses phosphates (génétique).
- MESH :
- déficit : N-Glycosyl hydrolases, Purine nucleoside phosphorylase.
- génétique : AMP-Activated Protein Kinases, Cyclic AMP-Dependent Protein Kinases, N-Glycosyl hydrolases, Protein-Serine-Threonine Kinases, Protéines de Saccharomyces cerevisiae, Purine nucleoside phosphorylase, Saccharomyces cerevisiae, Stress physiologique, Transaldolase, Voie des pentoses phosphates.
- métabolisme : AMP-Activated Protein Kinases, Cyclic AMP-Dependent Protein Kinases, Glycéraldéhyde 3-phosphate, NADP, Nucléotides, Protein-Serine-Threonine Kinases, Protéines de Saccharomyces cerevisiae, Ribose, Saccharomyces cerevisiae, Transaldolase.
- Oses phosphates, Régulation de l'expression des gènes fongiques, Transduction du signal.
English descriptors
- KwdEn :
- AMP-Activated Protein Kinases (genetics), AMP-Activated Protein Kinases (metabolism), Cyclic AMP-Dependent Protein Kinases (genetics), Cyclic AMP-Dependent Protein Kinases (metabolism), Gene Expression Regulation, Fungal (MeSH), Glyceraldehyde 3-Phosphate (metabolism), N-Glycosyl Hydrolases (deficiency), N-Glycosyl Hydrolases (genetics), NADP (metabolism), Nucleotides (metabolism), Pentose Phosphate Pathway (genetics), Protein-Serine-Threonine Kinases (genetics), Protein-Serine-Threonine Kinases (metabolism), Purine-Nucleoside Phosphorylase (deficiency), Purine-Nucleoside Phosphorylase (genetics), Ribose (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (MeSH), Stress, Physiological (genetics), Sugar Phosphates (MeSH), Transaldolase (genetics), Transaldolase (metabolism).
- MESH :
- chemical , deficiency : N-Glycosyl Hydrolases, Purine-Nucleoside Phosphorylase.
- chemical , genetics : AMP-Activated Protein Kinases, Cyclic AMP-Dependent Protein Kinases, N-Glycosyl Hydrolases, Protein-Serine-Threonine Kinases, Purine-Nucleoside Phosphorylase, Saccharomyces cerevisiae Proteins, Transaldolase.
- chemical , metabolism : AMP-Activated Protein Kinases, Cyclic AMP-Dependent Protein Kinases, Glyceraldehyde 3-Phosphate, NADP, Nucleotides, Protein-Serine-Threonine Kinases, Ribose, Saccharomyces cerevisiae Proteins, Transaldolase.
- genetics : Pentose Phosphate Pathway, Saccharomyces cerevisiae, Stress, Physiological.
- metabolism : Saccharomyces cerevisiae.
- Gene Expression Regulation, Fungal, Signal Transduction, Sugar Phosphates.
Abstract
Nucleotide degradation is a universal metabolic capability. Here we combine metabolomics, genetics and biochemistry to characterize the yeast pathway. Nutrient starvation, via PKA, AMPK/SNF1, and TOR, triggers autophagic breakdown of ribosomes into nucleotides. A protein not previously associated with nucleotide degradation, Phm8, converts nucleotide monophosphates into nucleosides. Downstream steps, which involve the purine nucleoside phosphorylase, Pnp1, and pyrimidine nucleoside hydrolase, Urh1, funnel ribose into the nonoxidative pentose phosphate pathway. During carbon starvation, the ribose-derived carbon accumulates as sedoheptulose-7-phosphate, whose consumption by transaldolase is impaired due to depletion of transaldolase's other substrate, glyceraldehyde-3-phosphate. Oxidative stress increases glyceraldehyde-3-phosphate, resulting in rapid consumption of sedoheptulose-7-phosphate to make NADPH for antioxidant defense. Ablation of Phm8 or double deletion of Pnp1 and Urh1 prevent effective nucleotide salvage, resulting in metabolite depletion and impaired survival of starving yeast. Thus, ribose salvage provides means of surviving nutrient starvation and oxidative stress.
DOI: 10.1038/msb.2013.21
PubMed: 23670538
PubMed Central: PMC4039369
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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xml:lang="en"><term>Pentose Phosphate Pathway</term><term>Saccharomyces cerevisiae</term><term>Stress, Physiological</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>AMP-Activated Protein Kinases</term><term>Cyclic AMP-Dependent Protein Kinases</term><term>N-Glycosyl hydrolases</term><term>Protein-Serine-Threonine Kinases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Purine nucleoside phosphorylase</term><term>Saccharomyces cerevisiae</term><term>Stress physiologique</term><term>Transaldolase</term><term>Voie des pentoses phosphates</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>AMP-Activated Protein Kinases</term><term>Cyclic AMP-Dependent Protein Kinases</term><term>Glycéraldéhyde 3-phosphate</term><term>NADP</term><term>Nucléotides</term><term>Protein-Serine-Threonine Kinases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Ribose</term><term>Saccharomyces cerevisiae</term><term>Transaldolase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Gene Expression Regulation, Fungal</term><term>Signal Transduction</term><term>Sugar Phosphates</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Oses phosphates</term><term>Régulation de l'expression des gènes fongiques</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Nucleotide degradation is a universal metabolic capability. Here we combine metabolomics, genetics and biochemistry to characterize the yeast pathway. Nutrient starvation, via PKA, AMPK/SNF1, and TOR, triggers autophagic breakdown of ribosomes into nucleotides. A protein not previously associated with nucleotide degradation, Phm8, converts nucleotide monophosphates into nucleosides. Downstream steps, which involve the purine nucleoside phosphorylase, Pnp1, and pyrimidine nucleoside hydrolase, Urh1, funnel ribose into the nonoxidative pentose phosphate pathway. During carbon starvation, the ribose-derived carbon accumulates as sedoheptulose-7-phosphate, whose consumption by transaldolase is impaired due to depletion of transaldolase's other substrate, glyceraldehyde-3-phosphate. Oxidative stress increases glyceraldehyde-3-phosphate, resulting in rapid consumption of sedoheptulose-7-phosphate to make NADPH for antioxidant defense. Ablation of Phm8 or double deletion of Pnp1 and Urh1 prevent effective nucleotide salvage, resulting in metabolite depletion and impaired survival of starving yeast. Thus, ribose salvage provides means of surviving nutrient starvation and oxidative stress.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23670538</PMID><DateCompleted><Year>2013</Year><Month>09</Month><Day>13</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1744-4292</ISSN><JournalIssue CitedMedium="Internet"><Volume>9</Volume><PubDate><Year>2013</Year><Month>May</Month><Day>14</Day></PubDate></JournalIssue><Title>Molecular systems biology</Title><ISOAbbreviation>Mol Syst Biol</ISOAbbreviation></Journal><ArticleTitle>Nucleotide degradation and ribose salvage in yeast.</ArticleTitle><Pagination><MedlinePgn>665</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/msb.2013.21</ELocationID><Abstract><AbstractText>Nucleotide degradation is a universal metabolic capability. Here we combine metabolomics, genetics and biochemistry to characterize the yeast pathway. Nutrient starvation, via PKA, AMPK/SNF1, and TOR, triggers autophagic breakdown of ribosomes into nucleotides. A protein not previously associated with nucleotide degradation, Phm8, converts nucleotide monophosphates into nucleosides. Downstream steps, which involve the purine nucleoside phosphorylase, Pnp1, and pyrimidine nucleoside hydrolase, Urh1, funnel ribose into the nonoxidative pentose phosphate pathway. During carbon starvation, the ribose-derived carbon accumulates as sedoheptulose-7-phosphate, whose consumption by transaldolase is impaired due to depletion of transaldolase's other substrate, glyceraldehyde-3-phosphate. Oxidative stress increases glyceraldehyde-3-phosphate, resulting in rapid consumption of sedoheptulose-7-phosphate to make NADPH for antioxidant defense. Ablation of Phm8 or double deletion of Pnp1 and Urh1 prevent effective nucleotide salvage, resulting in metabolite depletion and impaired survival of starving yeast. Thus, ribose salvage provides means of surviving nutrient starvation and oxidative stress.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Xu</LastName><ForeName>Yi-Fan</ForeName><Initials>YF</Initials><AffiliationInfo><Affiliation>Lewis Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Létisse</LastName><ForeName>Fabien</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Absalan</LastName><ForeName>Farnaz</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Lu</LastName><ForeName>Wenyun</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Kuznetsova</LastName><ForeName>Ekaterina</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Brown</LastName><ForeName>Greg</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Caudy</LastName><ForeName>Amy A</ForeName><Initials>AA</Initials></Author><Author ValidYN="Y"><LastName>Yakunin</LastName><ForeName>Alexander F</ForeName><Initials>AF</Initials></Author><Author ValidYN="Y"><LastName>Broach</LastName><ForeName>James R</ForeName><Initials>JR</Initials></Author><Author ValidYN="Y"><LastName>Rabinowitz</LastName><ForeName>Joshua D</ForeName><Initials>JD</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>P50 GM071508</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 CA163591</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM076562</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>CA163591</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>05</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Mol Syst Biol</MedlineTA><NlmUniqueID>101235389</NlmUniqueID><ISSNLinking>1744-4292</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009711">Nucleotides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013403">Sugar Phosphates</NameOfSubstance></Chemical><Chemical><RegistryNumber>142-10-9</RegistryNumber><NameOfSubstance UI="D005986">Glyceraldehyde 3-Phosphate</NameOfSubstance></Chemical><Chemical><RegistryNumber>2646-35-7</RegistryNumber><NameOfSubstance UI="C020495">sedoheptulose 7-phosphate</NameOfSubstance></Chemical><Chemical><RegistryNumber>53-59-8</RegistryNumber><NameOfSubstance UI="D009249">NADP</NameOfSubstance></Chemical><Chemical><RegistryNumber>681HV46001</RegistryNumber><NameOfSubstance UI="D012266">Ribose</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.2.1.2</RegistryNumber><NameOfSubstance UI="D014153">Transaldolase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.4.2.1</RegistryNumber><NameOfSubstance UI="D011683">Purine-Nucleoside Phosphorylase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="C071570">SNF1-related protein kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="C500749">target of rapamycin protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.11</RegistryNumber><NameOfSubstance UI="D017868">Cyclic AMP-Dependent Protein Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.31</RegistryNumber><NameOfSubstance UI="D055372">AMP-Activated Protein Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.2.-</RegistryNumber><NameOfSubstance UI="D009699">N-Glycosyl Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.2.3</RegistryNumber><NameOfSubstance UI="C454867">URH1 protein, S cerevisiae</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D055372" MajorTopicYN="N">AMP-Activated Protein Kinases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017868" MajorTopicYN="N">Cyclic AMP-Dependent Protein Kinases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="Y">Gene Expression Regulation, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005986" MajorTopicYN="N">Glyceraldehyde 3-Phosphate</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009699" MajorTopicYN="N">N-Glycosyl Hydrolases</DescriptorName><QualifierName UI="Q000172" MajorTopicYN="N">deficiency</QualifierName><QualifierName UI="Q000235" 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