Calculation of the relative metastabilities of proteins in subcellular compartments of Saccharomyces cerevisiae.
Identifieur interne : 000B46 ( Main/Exploration ); précédent : 000B45; suivant : 000B47Calculation of the relative metastabilities of proteins in subcellular compartments of Saccharomyces cerevisiae.
Auteurs : Jeffrey M. Dick [États-Unis]Source :
- BMC systems biology [ 1752-0509 ] ; 2009.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Oxygen, Saccharomyces cerevisiae Proteins.
- metabolism : Intracellular Space, Saccharomyces cerevisiae.
- Electrochemical Techniques, Oxidation-Reduction, Systems Biology, Thermodynamics.
Abstract
BACKGROUND
Protein subcellular localization and differences in oxidation state between subcellular compartments are two well-studied features of the the cellular organization of S. cerevisiae (yeast). Theories about the origin of subcellular organization are assisted by computational models that can integrate data from observations of compositional and chemical properties of the system. PRESENTATION AND IMPLICATIONS OF THE HYPOTHESIS: I adopt the hypothesis that the state of yeast subcellular organization is in a local energy minimum. This hypothesis implies that equilibrium thermodynamic models can yield predictions about the interdependence between populations of proteins and their subcellular chemical environments.
TESTING THE HYPOTHESIS
Three types of tests are proposed. First, there should be correlations between modeled and observed oxidation states for different compartments. Second, there should be a correspondence between the energy requirements of protein formation and the order the appearance of organelles during cellular development. Third, there should be correlations between the predicted and observed relative abundances of interacting proteins within compartments.
RESULTS
The relative metastability fields of subcellular homologs of glutaredoxin and thioredoxin indicate a trend from less to more oxidizing as mitochondrion - cytoplasm - nucleus. Representing the overall amino acid compositions of proteins in 23 different compartments each with a single reference model protein suggests that the formation reactions for proteins in the vacuole (in relatively oxidizing conditions), ER and early Golgi (in relatively reducing conditions) are relatively highly favored, while that for the microtubule is the most costly. The relative abundances of model proteins for each compartment inferred from experimental data were found in some cases to correlate with the predicted abundances, and both positive and negative correlations were found for some assemblages of proteins in known complexes.
CONCLUSION
The results of these calculations and tests suggest that a tendency toward a metastable energy minimum could underlie some organizational links between the the chemical thermodynamic properties of proteins and subcellular chemical environments. Future models of this kind will benefit from consideration of additional thermodynamic variables together with more detailed subcellular observations.
DOI: 10.1186/1752-0509-3-75
PubMed: 19615086
PubMed Central: PMC2734844
Affiliations:
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Dick</name><affiliation wicri:level="2"><nlm:affiliation>Department of Earth and Planetary Science, University of California, 307 McCone Hall, #4767 Berkeley, CA 94720-4767, USA. jedick@berkeley.edu</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Earth and Planetary Science, University of California, 307 McCone Hall, #4767 Berkeley, CA 94720-4767</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19615086</idno><idno type="pmid">19615086</idno><idno type="doi">10.1186/1752-0509-3-75</idno><idno type="pmc">PMC2734844</idno><idno type="wicri:Area/Main/Corpus">000A91</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000A91</idno><idno type="wicri:Area/Main/Curation">000A91</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000A91</idno><idno type="wicri:Area/Main/Exploration">000A91</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Calculation of the relative metastabilities of proteins in subcellular compartments of Saccharomyces cerevisiae.</title><author><name sortKey="Dick, Jeffrey M" sort="Dick, Jeffrey M" uniqKey="Dick J" first="Jeffrey M" last="Dick">Jeffrey M. Dick</name><affiliation wicri:level="2"><nlm:affiliation>Department of Earth and Planetary Science, University of California, 307 McCone Hall, #4767 Berkeley, CA 94720-4767, USA. jedick@berkeley.edu</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Earth and Planetary Science, University of California, 307 McCone Hall, #4767 Berkeley, CA 94720-4767</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author></analytic><series><title level="j">BMC systems biology</title><idno type="eISSN">1752-0509</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Electrochemical Techniques (MeSH)</term><term>Intracellular Space (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxygen (metabolism)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Systems Biology (MeSH)</term><term>Thermodynamics (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Biologie des systèmes (MeSH)</term><term>Espace intracellulaire (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Oxygène (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Techniques électrochimiques (MeSH)</term><term>Thermodynamique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Oxygen</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Intracellular Space</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Espace intracellulaire</term><term>Oxygène</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electrochemical Techniques</term><term>Oxidation-Reduction</term><term>Systems Biology</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biologie des systèmes</term><term>Oxydoréduction</term><term>Techniques électrochimiques</term><term>Thermodynamique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>BACKGROUND</b></p><p>Protein subcellular localization and differences in oxidation state between subcellular compartments are two well-studied features of the the cellular organization of S. cerevisiae (yeast). Theories about the origin of subcellular organization are assisted by computational models that can integrate data from observations of compositional and chemical properties of the system. PRESENTATION AND IMPLICATIONS OF THE HYPOTHESIS: I adopt the hypothesis that the state of yeast subcellular organization is in a local energy minimum. This hypothesis implies that equilibrium thermodynamic models can yield predictions about the interdependence between populations of proteins and their subcellular chemical environments.</p></div><div type="abstract" xml:lang="en"><p><b>TESTING THE HYPOTHESIS</b></p><p>Three types of tests are proposed. First, there should be correlations between modeled and observed oxidation states for different compartments. Second, there should be a correspondence between the energy requirements of protein formation and the order the appearance of organelles during cellular development. Third, there should be correlations between the predicted and observed relative abundances of interacting proteins within compartments.</p></div><div type="abstract" xml:lang="en"><p><b>RESULTS</b></p><p>The relative metastability fields of subcellular homologs of glutaredoxin and thioredoxin indicate a trend from less to more oxidizing as mitochondrion - cytoplasm - nucleus. Representing the overall amino acid compositions of proteins in 23 different compartments each with a single reference model protein suggests that the formation reactions for proteins in the vacuole (in relatively oxidizing conditions), ER and early Golgi (in relatively reducing conditions) are relatively highly favored, while that for the microtubule is the most costly. The relative abundances of model proteins for each compartment inferred from experimental data were found in some cases to correlate with the predicted abundances, and both positive and negative correlations were found for some assemblages of proteins in known complexes.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSION</b></p><p>The results of these calculations and tests suggest that a tendency toward a metastable energy minimum could underlie some organizational links between the the chemical thermodynamic properties of proteins and subcellular chemical environments. Future models of this kind will benefit from consideration of additional thermodynamic variables together with more detailed subcellular observations.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19615086</PMID><DateCompleted><Year>2009</Year><Month>10</Month><Day>01</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1752-0509</ISSN><JournalIssue CitedMedium="Internet"><Volume>3</Volume><PubDate><Year>2009</Year><Month>Jul</Month><Day>18</Day></PubDate></JournalIssue><Title>BMC systems biology</Title><ISOAbbreviation>BMC Syst Biol</ISOAbbreviation></Journal><ArticleTitle>Calculation of the relative metastabilities of proteins in subcellular compartments of Saccharomyces cerevisiae.</ArticleTitle><Pagination><MedlinePgn>75</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1186/1752-0509-3-75</ELocationID><Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Protein subcellular localization and differences in oxidation state between subcellular compartments are two well-studied features of the the cellular organization of S. cerevisiae (yeast). Theories about the origin of subcellular organization are assisted by computational models that can integrate data from observations of compositional and chemical properties of the system. PRESENTATION AND IMPLICATIONS OF THE HYPOTHESIS: I adopt the hypothesis that the state of yeast subcellular organization is in a local energy minimum. This hypothesis implies that equilibrium thermodynamic models can yield predictions about the interdependence between populations of proteins and their subcellular chemical environments.</AbstractText><AbstractText Label="TESTING THE HYPOTHESIS" NlmCategory="METHODS">Three types of tests are proposed. First, there should be correlations between modeled and observed oxidation states for different compartments. Second, there should be a correspondence between the energy requirements of protein formation and the order the appearance of organelles during cellular development. Third, there should be correlations between the predicted and observed relative abundances of interacting proteins within compartments.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">The relative metastability fields of subcellular homologs of glutaredoxin and thioredoxin indicate a trend from less to more oxidizing as mitochondrion - cytoplasm - nucleus. Representing the overall amino acid compositions of proteins in 23 different compartments each with a single reference model protein suggests that the formation reactions for proteins in the vacuole (in relatively oxidizing conditions), ER and early Golgi (in relatively reducing conditions) are relatively highly favored, while that for the microtubule is the most costly. The relative abundances of model proteins for each compartment inferred from experimental data were found in some cases to correlate with the predicted abundances, and both positive and negative correlations were found for some assemblages of proteins in known complexes.</AbstractText><AbstractText Label="CONCLUSION" NlmCategory="CONCLUSIONS">The results of these calculations and tests suggest that a tendency toward a metastable energy minimum could underlie some organizational links between the the chemical thermodynamic properties of proteins and subcellular chemical environments. 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