1 Ocak 2009 Dergi makalesi Açık Erişim

Bektas, Muhammet; Varol, Basak; Nurten, Ruestem; Bermek, Engin

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  <identifier identifierType="URL">https://aperta.ulakbim.gov.tr/record/41765</identifier>
  <creators>
    <creator>
      <creatorName>Bektas, Muhammet</creatorName>
      <givenName>Muhammet</givenName>
      <familyName>Bektas</familyName>
      <affiliation>Istanbul Univ, Dept Biophys, Istanbul Fac Med, Istanbul, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Varol, Basak</creatorName>
      <givenName>Basak</givenName>
      <familyName>Varol</familyName>
      <affiliation>Istanbul Univ, Dept Biophys, Istanbul Fac Med, Istanbul, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Nurten, Ruestem</creatorName>
      <givenName>Ruestem</givenName>
      <familyName>Nurten</familyName>
      <affiliation>Istanbul Univ, Dept Biophys, Istanbul Fac Med, Istanbul, Turkey</affiliation>
    </creator>
    <creator>
      <creatorName>Bermek, Engin</creatorName>
      <givenName>Engin</givenName>
      <familyName>Bermek</familyName>
      <affiliation>Istanbul Univ, Dept Biophys, Istanbul Fac Med, Istanbul, Turkey</affiliation>
    </creator>
  </creators>
  <titles>
    <title>Interaction Of Diphtheria Toxin (Fragment A) With Actin</title>
  </titles>
  <publisher>Aperta</publisher>
  <publicationYear>2009</publicationYear>
  <dates>
    <date dateType="Issued">2009-01-01</date>
  </dates>
  <resourceType resourceTypeGeneral="Text">Journal article</resourceType>
  <alternateIdentifiers>
    <alternateIdentifier alternateIdentifierType="url">https://aperta.ulakbim.gov.tr/record/41765</alternateIdentifier>
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  <relatedIdentifiers>
    <relatedIdentifier relatedIdentifierType="DOI" relationType="IsIdenticalTo">10.1002/cbf.1590</relatedIdentifier>
  </relatedIdentifiers>
  <rightsList>
    <rights rightsURI="http://www.opendefinition.org/licenses/cc-by">Creative Commons Attribution</rights>
    <rights rightsURI="info:eu-repo/semantics/openAccess">Open Access</rights>
  </rightsList>
  <descriptions>
    <description descriptionType="Abstract">It was shown by gel filtration and viscosity measurements that N-terminal fragment (FA) of diphtheria toxin (DT) can interact with both G- and F-actin (filamentous actin). Elution profiles on Sephadex G- 100 indicated the formation of a binary complex of fragment A (FA) with globular actin monomer (G-actin), which was inhibited by gelsolin. Deoxyribonuclease I (DNase I) in turn appeared to interact with this complex. Tritiated FA was found to bind to F-actin stoichiometrically. This binding was inhibited again by gelsolin and G-actin, but not by DNase I. The binding of FA inhibited polymerization of G-actin and induced a time-dependent breakdown of F-actin under polymerization conditions. Inhibition of its ADP-ribosyltransferase activity did not have any effect on the interactions of FA with actin. FA interacted with actin also in the cell. After treatment of human umbilical vein endothelial cells (HUVEC) with biotin-labeled DT, Western blot analysis revealed predominantly the presence of actin in affinity-isolated complexes of the labeled FA. Similarly, FA was found in immunoaffinity-isolated complexes of actin. Copyright (C) 2009 John Wiley &amp;amp; Sons, Ltd.</description>
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