The ADP-ribosylation of Sulfolobus solfataricus Sso7 modulates protein/DNA interactions in vitro.
Identifieur interne : 000676 ( Ncbi/Merge ); précédent : 000675; suivant : 000677The ADP-ribosylation of Sulfolobus solfataricus Sso7 modulates protein/DNA interactions in vitro.
Auteurs : Sabrina Castellano [Italie] ; Benedetta Farina ; Maria Rosaria Faraone-MennellaSource :
- FEBS letters [ 1873-3468 ] ; 2009.
Descripteurs français
- KwdFr :
- ADN des archées (métabolisme), ADP (métabolisme), Maturation post-traductionnelle des protéines (physiologie), Poly(ADP-ribose) polymerases (métabolisme), Protéines d'archée (métabolisme), Protéines de liaison à l'ADN (métabolisme), Structure tertiaire des protéines (physiologie), Sulfolobus solfataricus (métabolisme).
- MESH :
English descriptors
- KwdEn :
- Adenosine Diphosphate (metabolism), Archaeal Proteins (metabolism), DNA, Archaeal (metabolism), DNA-Binding Proteins (metabolism), Poly(ADP-ribose) Polymerases (metabolism), Protein Processing, Post-Translational (physiology), Protein Structure, Tertiary (physiology), Sulfolobus solfataricus (metabolism).
- MESH :
- chemical , metabolism : Adenosine Diphosphate, Archaeal Proteins, DNA, Archaeal, DNA-Binding Proteins, Poly(ADP-ribose) Polymerases.
- metabolism : Sulfolobus solfataricus.
- physiology : Protein Processing, Post-Translational, Protein Structure, Tertiary.
Abstract
The 7 kDa Sso7 is a basic protein particularly abundant in Sulfolobus solfataricus and is involved in DNA assembly. This protein undergoes in vitro ADP-ribosylation by an endogenous poly(ADP-ribose) polymerase-like enzyme. The circular dichroism spectrum of purified ADP-ribosylated Sso7 shows that this modification stabilizes the prevalent protein beta-conformation, as suggested by shifting of negative ellipticity minimum to 220 nm. Moreover, a short ADP-ribose chain (up to 6-mers) bound to Sso7 is able to reduce drastically the thermoprotective and DNA condensing ability of the protein, suggesting a possible regulatory role of ADP-ribosylation in sulfolobal DNA organization.
DOI: 10.1016/j.febslet.2009.03.003
PubMed: 19272378
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Angelo, Napoli</wicri:regionArea><wicri:noRegion>Napoli</wicri:noRegion></affiliation></author><author><name sortKey="Farina, Benedetta" sort="Farina, Benedetta" uniqKey="Farina B" first="Benedetta" last="Farina">Benedetta Farina</name></author><author><name sortKey="Faraone Mennella, Maria Rosaria" sort="Faraone Mennella, Maria Rosaria" uniqKey="Faraone Mennella M" first="Maria Rosaria" last="Faraone-Mennella">Maria Rosaria Faraone-Mennella</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19272378</idno><idno type="pmid">19272378</idno><idno type="doi">10.1016/j.febslet.2009.03.003</idno><idno type="wicri:Area/PubMed/Corpus">002026</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002026</idno><idno type="wicri:Area/PubMed/Curation">002026</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002026</idno><idno type="wicri:Area/PubMed/Checkpoint">001E80</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001E80</idno><idno type="wicri:Area/Ncbi/Merge">000676</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The ADP-ribosylation of Sulfolobus solfataricus Sso7 modulates protein/DNA interactions in vitro.</title><author><name sortKey="Castellano, Sabrina" sort="Castellano, Sabrina" uniqKey="Castellano S" first="Sabrina" last="Castellano">Sabrina Castellano</name><affiliation wicri:level="1"><nlm:affiliation>Department of Structural and Functional Biology, Faculty of Sciences MM FF NN, University of Naples Federico II, Complesso Universitario di Monte S. Angelo, Napoli, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Structural and Functional Biology, Faculty of Sciences MM FF NN, University of Naples Federico II, Complesso Universitario di Monte S. Angelo, Napoli</wicri:regionArea><wicri:noRegion>Napoli</wicri:noRegion></affiliation></author><author><name sortKey="Farina, Benedetta" sort="Farina, Benedetta" uniqKey="Farina B" first="Benedetta" last="Farina">Benedetta Farina</name></author><author><name sortKey="Faraone Mennella, Maria Rosaria" sort="Faraone Mennella, Maria Rosaria" uniqKey="Faraone Mennella M" first="Maria Rosaria" last="Faraone-Mennella">Maria Rosaria Faraone-Mennella</name></author></analytic><series><title level="j">FEBS letters</title><idno type="eISSN">1873-3468</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Diphosphate (metabolism)</term><term>Archaeal Proteins (metabolism)</term><term>DNA, Archaeal (metabolism)</term><term>DNA-Binding Proteins (metabolism)</term><term>Poly(ADP-ribose) Polymerases (metabolism)</term><term>Protein Processing, Post-Translational (physiology)</term><term>Protein Structure, Tertiary (physiology)</term><term>Sulfolobus solfataricus (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN des archées (métabolisme)</term><term>ADP (métabolisme)</term><term>Maturation post-traductionnelle des protéines (physiologie)</term><term>Poly(ADP-ribose) polymerases (métabolisme)</term><term>Protéines d'archée (métabolisme)</term><term>Protéines de liaison à l'ADN (métabolisme)</term><term>Structure tertiaire des protéines (physiologie)</term><term>Sulfolobus solfataricus (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Diphosphate</term><term>Archaeal Proteins</term><term>DNA, Archaeal</term><term>DNA-Binding Proteins</term><term>Poly(ADP-ribose) Polymerases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Sulfolobus solfataricus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ADN des archées</term><term>ADP</term><term>Poly(ADP-ribose) polymerases</term><term>Protéines d'archée</term><term>Protéines de liaison à l'ADN</term><term>Sulfolobus solfataricus</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Maturation post-traductionnelle des protéines</term><term>Structure tertiaire des protéines</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Protein Processing, Post-Translational</term><term>Protein Structure, Tertiary</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The 7 kDa Sso7 is a basic protein particularly abundant in Sulfolobus solfataricus and is involved in DNA assembly. This protein undergoes in vitro ADP-ribosylation by an endogenous poly(ADP-ribose) polymerase-like enzyme. The circular dichroism spectrum of purified ADP-ribosylated Sso7 shows that this modification stabilizes the prevalent protein beta-conformation, as suggested by shifting of negative ellipticity minimum to 220 nm. Moreover, a short ADP-ribose chain (up to 6-mers) bound to Sso7 is able to reduce drastically the thermoprotective and DNA condensing ability of the protein, suggesting a possible regulatory role of ADP-ribosylation in sulfolobal DNA organization.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19272378</PMID><DateCompleted><Year>2009</Year><Month>04</Month><Day>14</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-3468</ISSN><JournalIssue CitedMedium="Internet"><Volume>583</Volume><Issue>7</Issue><PubDate><Year>2009</Year><Month>Apr</Month><Day>02</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett.</ISOAbbreviation></Journal><ArticleTitle>The ADP-ribosylation of Sulfolobus solfataricus Sso7 modulates protein/DNA interactions in vitro.</ArticleTitle><Pagination><MedlinePgn>1154-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.febslet.2009.03.003</ELocationID><Abstract><AbstractText>The 7 kDa Sso7 is a basic protein particularly abundant in Sulfolobus solfataricus and is involved in DNA assembly. This protein undergoes in vitro ADP-ribosylation by an endogenous poly(ADP-ribose) polymerase-like enzyme. The circular dichroism spectrum of purified ADP-ribosylated Sso7 shows that this modification stabilizes the prevalent protein beta-conformation, as suggested by shifting of negative ellipticity minimum to 220 nm. Moreover, a short ADP-ribose chain (up to 6-mers) bound to Sso7 is able to reduce drastically the thermoprotective and DNA condensing ability of the protein, suggesting a possible regulatory role of ADP-ribosylation in sulfolobal DNA organization.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Castellano</LastName><ForeName>Sabrina</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Structural and Functional Biology, Faculty of Sciences MM FF NN, University of Naples Federico II, Complesso Universitario di Monte S. Angelo, Napoli, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Farina</LastName><ForeName>Benedetta</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Faraone-Mennella</LastName><ForeName>Maria Rosaria</ForeName><Initials>MR</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2009</Year><Month>03</Month><Day>09</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="D019843">Archaeal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019641">DNA, Archaeal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004268">DNA-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C093228">Sso7d protein, Sulfolobus</NameOfSubstance></Chemical><Chemical><RegistryNumber>61D2G4IYVH</RegistryNumber><NameOfSubstance UI="D000244">Adenosine Diphosphate</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.4.2.30</RegistryNumber><NameOfSubstance UI="D011065">Poly(ADP-ribose) Polymerases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000244" MajorTopicYN="N">Adenosine Diphosphate</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019843" MajorTopicYN="N">Archaeal Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019641" MajorTopicYN="N">DNA, Archaeal</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004268" MajorTopicYN="N">DNA-Binding Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011065" MajorTopicYN="N">Poly(ADP-ribose) Polymerases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011499" MajorTopicYN="N">Protein Processing, Post-Translational</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D048229" MajorTopicYN="N">Sulfolobus solfataricus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2009</Year><Month>02</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2009</Year><Month>02</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2009</Year><Month>03</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>3</Month><Day>11</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>3</Month><Day>11</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>4</Month><Day>15</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19272378</ArticleId><ArticleId IdType="pii">S0014-5793(09)00174-4</ArticleId><ArticleId IdType="doi">10.1016/j.febslet.2009.03.003</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Italie</li></country></list><tree><noCountry><name sortKey="Faraone Mennella, Maria Rosaria" sort="Faraone Mennella, Maria Rosaria" uniqKey="Faraone Mennella M" first="Maria Rosaria" last="Faraone-Mennella">Maria Rosaria Faraone-Mennella</name><name sortKey="Farina, Benedetta" sort="Farina, Benedetta" uniqKey="Farina B" first="Benedetta" last="Farina">Benedetta Farina</name></noCountry><country name="Italie"><noRegion><name sortKey="Castellano, Sabrina" sort="Castellano, Sabrina" uniqKey="Castellano S" first="Sabrina" last="Castellano">Sabrina Castellano</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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