Complex formation between recombinant ATP sulfurylase and APS reductase of Allium cepa (L.).
Identifieur interne : 000C93 ( Main/Exploration ); précédent : 000C92; suivant : 000C94Complex formation between recombinant ATP sulfurylase and APS reductase of Allium cepa (L.).
Auteurs : Mathew Cumming [Nouvelle-Zélande] ; Susanna Leung ; John Mccallum ; Michael T. McmanusSource :
- FEBS letters [ 0014-5793 ] ; 2007.
Descripteurs français
- KwdFr :
- Données de séquences moléculaires (MeSH), Dosage immunologique (MeSH), Escherichia coli (MeSH), Immunoprécipitation (MeSH), Liaison aux protéines (MeSH), Ligands (MeSH), Oignons (enzymologie), Oxidoreductases acting on sulfur group donors (composition chimique), Oxidoreductases acting on sulfur group donors (métabolisme), Protéines recombinantes (métabolisme), Spécificité du substrat (MeSH), Sulfate adenylyltransferase (composition chimique), Sulfate adenylyltransferase (métabolisme), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Oxidoreductases acting on sulfur group donors, Sulfate adenylyltransferase.
- enzymologie : Oignons.
- métabolisme : Oxidoreductases acting on sulfur group donors, Protéines recombinantes, Sulfate adenylyltransferase.
- Données de séquences moléculaires, Dosage immunologique, Escherichia coli, Immunoprécipitation, Liaison aux protéines, Ligands, Spécificité du substrat, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Escherichia coli (MeSH), Immunoassay (MeSH), Immunoprecipitation (MeSH), Ligands (MeSH), Molecular Sequence Data (MeSH), Onions (enzymology), Oxidoreductases Acting on Sulfur Group Donors (chemistry), Oxidoreductases Acting on Sulfur Group Donors (metabolism), Protein Binding (MeSH), Recombinant Proteins (metabolism), Substrate Specificity (MeSH), Sulfate Adenylyltransferase (chemistry), Sulfate Adenylyltransferase (metabolism).
- MESH :
- chemical , chemistry : Oxidoreductases Acting on Sulfur Group Donors, Sulfate Adenylyltransferase.
- chemical , metabolism : Oxidoreductases Acting on Sulfur Group Donors, Recombinant Proteins, Sulfate Adenylyltransferase.
- chemical : Ligands.
- enzymology : Onions.
- Amino Acid Sequence, Escherichia coli, Immunoassay, Immunoprecipitation, Molecular Sequence Data, Protein Binding, Substrate Specificity.
Abstract
Recombinant ATP sulfurylase (AcATPS1) and adenosine-5'-phosphosulfate reductase (AcAPR1) from Allium cepa have been used to determine if these enzymes form protein-protein complexes in vitro. Using a solid phase binding assay, AcAPR1 was shown to interact with AcATPS1. The AcAPR1 enzyme was also expressed in E. coli as the N-terminal reductase domain (AcAPR1-N) and the C-terminal glutaredoxin domain (AcAPR1-C), but neither of these truncated proteins interacted with AcATPS1. The solid-phase interactions were confirmed by immune-precipitation, where anti-AcATPS1 IgG precipitated the full-length AcAPR1 protein, but not AcAPR1-N and AcAPR1-C. Finally, using the ligand binding assay, full-length AcATPS1 has been shown to bind to membrane-localised full-length AcAPR1. The significance of an interaction between chloroplastidic ATPS and APR in A. cepa is evaluated with respect to the control of the reductive assimilation of sulfate.
DOI: 10.1016/j.febslet.2007.07.062
PubMed: 17692849
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Using a solid phase binding assay, AcAPR1 was shown to interact with AcATPS1. The AcAPR1 enzyme was also expressed in E. coli as the N-terminal reductase domain (AcAPR1-N) and the C-terminal glutaredoxin domain (AcAPR1-C), but neither of these truncated proteins interacted with AcATPS1. The solid-phase interactions were confirmed by immune-precipitation, where anti-AcATPS1 IgG precipitated the full-length AcAPR1 protein, but not AcAPR1-N and AcAPR1-C. Finally, using the ligand binding assay, full-length AcATPS1 has been shown to bind to membrane-localised full-length AcAPR1. The significance of an interaction between chloroplastidic ATPS and APR in A. cepa is evaluated with respect to the control of the reductive assimilation of sulfate.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17692849</PMID><DateCompleted><Year>2007</Year><Month>10</Month><Day>19</Day></DateCompleted><DateRevised><Year>2007</Year><Month>08</Month><Day>28</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>581</Volume><Issue>22</Issue><PubDate><Year>2007</Year><Month>Sep</Month><Day>04</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Complex formation between recombinant ATP sulfurylase and APS reductase of Allium cepa (L.).</ArticleTitle><Pagination><MedlinePgn>4139-47</MedlinePgn></Pagination><Abstract><AbstractText>Recombinant ATP sulfurylase (AcATPS1) and adenosine-5'-phosphosulfate reductase (AcAPR1) from Allium cepa have been used to determine if these enzymes form protein-protein complexes in vitro. Using a solid phase binding assay, AcAPR1 was shown to interact with AcATPS1. The AcAPR1 enzyme was also expressed in E. coli as the N-terminal reductase domain (AcAPR1-N) and the C-terminal glutaredoxin domain (AcAPR1-C), but neither of these truncated proteins interacted with AcATPS1. The solid-phase interactions were confirmed by immune-precipitation, where anti-AcATPS1 IgG precipitated the full-length AcAPR1 protein, but not AcAPR1-N and AcAPR1-C. Finally, using the ligand binding assay, full-length AcATPS1 has been shown to bind to membrane-localised full-length AcAPR1. The significance of an interaction between chloroplastidic ATPS and APR in A. cepa is evaluated with respect to the control of the reductive assimilation of sulfate.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Cumming</LastName><ForeName>Mathew</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Institute of Molecular Biosciences, Massey University, Private Bag 11-222, Palmerston North, New Zealand.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Leung</LastName><ForeName>Susanna</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>McCallum</LastName><ForeName>John</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>McManus</LastName><ForeName>Michael T</ForeName><Initials>MT</Initials></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>2007</Year><Month>08</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS Lett</MedlineTA><NlmUniqueID>0155157</NlmUniqueID><ISSNLinking>0014-5793</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008024">Ligands</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.-</RegistryNumber><NameOfSubstance UI="D050862">Oxidoreductases Acting on Sulfur Group Donors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.99.2</RegistryNumber><NameOfSubstance UI="C019618">adenylylsulfate reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.7.4</RegistryNumber><NameOfSubstance UI="D013430">Sulfate Adenylyltransferase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007118" MajorTopicYN="N">Immunoassay</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D047468" MajorTopicYN="N">Immunoprecipitation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008024" MajorTopicYN="N">Ligands</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019697" MajorTopicYN="N">Onions</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D050862" MajorTopicYN="N">Oxidoreductases Acting on Sulfur Group Donors</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013430" MajorTopicYN="N">Sulfate Adenylyltransferase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2007</Year><Month>05</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2007</Year><Month>07</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2007</Year><Month>07</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>8</Month><Day>19</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>10</Month><Day>20</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>8</Month><Day>19</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17692849</ArticleId><ArticleId IdType="pii">S0014-5793(07)00818-6</ArticleId><ArticleId IdType="doi">10.1016/j.febslet.2007.07.062</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Nouvelle-Zélande</li></country></list><tree><noCountry><name sortKey="Leung, Susanna" sort="Leung, Susanna" uniqKey="Leung S" first="Susanna" last="Leung">Susanna Leung</name><name sortKey="Mccallum, John" sort="Mccallum, John" uniqKey="Mccallum J" first="John" last="Mccallum">John Mccallum</name><name sortKey="Mcmanus, Michael T" sort="Mcmanus, Michael T" uniqKey="Mcmanus M" first="Michael T" last="Mcmanus">Michael T. Mcmanus</name></noCountry><country name="Nouvelle-Zélande"><noRegion><name sortKey="Cumming, Mathew" sort="Cumming, Mathew" uniqKey="Cumming M" first="Mathew" last="Cumming">Mathew Cumming</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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