<?xml version="1.0" encoding="utf-8"?>
<TEI xmlns="http://www.tei-c.org/ns/1.0" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:hal="http://hal.archives-ouvertes.fr/" xmlns:gml="http://www.opengis.net/gml/3.3/" xmlns:gmlce="http://www.opengis.net/gml/3.3/ce" version="1.1" xsi:schemaLocation="http://www.tei-c.org/ns/1.0 http://api.archives-ouvertes.fr/documents/aofr-sword.xsd">
  <teiHeader>
    <fileDesc>
      <titleStmt>
        <title>HAL TEI export of hal-03052799</title>
      </titleStmt>
      <publicationStmt>
        <distributor>CCSD</distributor>
        <availability status="restricted">
          <licence target="https://creativecommons.org/publicdomain/zero/1.0/">CC0 1.0 - Universal</licence>
        </availability>
        <date when="2026-05-18T03:58:55+02:00"/>
      </publicationStmt>
      <sourceDesc>
        <p part="N">HAL API Platform</p>
      </sourceDesc>
    </fileDesc>
  </teiHeader>
  <text>
    <body>
      <listBibl>
        <biblFull>
          <titleStmt>
            <title xml:lang="en">Impact of self-association on the architectural properties of bacterial nucleoid proteins</title>
            <author role="aut">
              <persName>
                <forename type="first">Marc</forename>
                <surname>Joyeux</surname>
              </persName>
              <email type="md5">f4139e9f6e01bca6419266e66198f9d0</email>
              <email type="domain">ujf-grenoble.fr</email>
              <idno type="idhal" notation="numeric">830376</idno>
              <idno type="halauthorid" notation="string">110457-830376</idno>
              <affiliation ref="#struct-1043294"/>
            </author>
            <editor role="depositor">
              <persName>
                <forename>Marc</forename>
                <surname>Joyeux</surname>
              </persName>
              <email type="md5">e2eea31d49375a2649406716514f31f6</email>
              <email type="domain">univ-grenoble-alpes.fr</email>
            </editor>
          </titleStmt>
          <editionStmt>
            <edition n="v1" type="current">
              <date type="whenSubmitted">2020-12-10 17:42:19</date>
              <date type="whenModified">2025-09-27 19:09:47</date>
              <date type="whenReleased">2020-12-18 13:34:52</date>
              <date type="whenProduced">2020</date>
              <date type="whenEndEmbargoed">2020-12-10</date>
              <ref type="file" target="https://hal.science/hal-03052799v1/document">
                <date notBefore="2020-12-10"/>
              </ref>
              <ref type="file" subtype="author" n="1" target="https://hal.science/hal-03052799v1/file/text_final_complet.pdf" id="file-3052799-2685969">
                <date notBefore="2020-12-10"/>
              </ref>
              <ref type="externalLink" target="https://hal.archives-ouvertes.fr/hal-03052799/file/text_final_complet.pdf"/>
            </edition>
            <respStmt>
              <resp>contributor</resp>
              <name key="103009">
                <persName>
                  <forename>Marc</forename>
                  <surname>Joyeux</surname>
                </persName>
                <email type="md5">e2eea31d49375a2649406716514f31f6</email>
                <email type="domain">univ-grenoble-alpes.fr</email>
              </name>
            </respStmt>
          </editionStmt>
          <publicationStmt>
            <distributor>CCSD</distributor>
            <idno type="halId">hal-03052799</idno>
            <idno type="halUri">https://hal.science/hal-03052799</idno>
            <idno type="halBibtex">joyeux:hal-03052799</idno>
            <idno type="halRefHtml">&lt;i&gt;Biophysical Journal&lt;/i&gt;, 2020, 120 (2), pp.370. &lt;a target="_blank" href="https://dx.doi.org/10.1016/j.bpj.2020.12.006"&gt;&amp;#x27E8;10.1016/j.bpj.2020.12.006&amp;#x27E9;&lt;/a&gt;</idno>
            <idno type="halRef">Biophysical Journal, 2020, 120 (2), pp.370. &amp;#x27E8;10.1016/j.bpj.2020.12.006&amp;#x27E9;</idno>
            <availability status="restricted">
              <licence target="https://about.hal.science/hal-authorisation-v1/">HAL Authorization<ref corresp="#file-3052799-2685969"/></licence>
            </availability>
          </publicationStmt>
          <seriesStmt>
            <idno type="stamp" n="UGA">HAL Grenoble Alpes</idno>
            <idno type="stamp" n="CNRS">CNRS - Centre national de la recherche scientifique</idno>
            <idno type="stamp" n="INPG">Institut polytechnique de Grenoble</idno>
            <idno type="stamp" n="LIPHY" corresp="CNRS">Laboratoire interdisciplinaire de Physique</idno>
            <idno type="stamp" n="UGA-EPE">Université Grenoble Alpes [2020-*]</idno>
            <idno type="stamp" n="TEST-UGA">TEST-UGA</idno>
          </seriesStmt>
          <notesStmt>
            <note type="audience" n="2">International</note>
            <note type="popular" n="0">No</note>
            <note type="peer" n="1">Yes</note>
          </notesStmt>
          <sourceDesc>
            <biblStruct>
              <analytic>
                <title xml:lang="en">Impact of self-association on the architectural properties of bacterial nucleoid proteins</title>
                <author role="aut">
                  <persName>
                    <forename type="first">Marc</forename>
                    <surname>Joyeux</surname>
                  </persName>
                  <email type="md5">f4139e9f6e01bca6419266e66198f9d0</email>
                  <email type="domain">ujf-grenoble.fr</email>
                  <idno type="idhal" notation="numeric">830376</idno>
                  <idno type="halauthorid" notation="string">110457-830376</idno>
                  <affiliation ref="#struct-1043294"/>
                </author>
              </analytic>
              <monogr>
                <idno type="halJournalId" status="VALID">11206</idno>
                <idno type="issn">0006-3495</idno>
                <idno type="eissn">1542-0086</idno>
                <title level="j">Biophysical Journal</title>
                <imprint>
                  <publisher>Biophysical Society</publisher>
                  <biblScope unit="volume">120</biblScope>
                  <biblScope unit="issue">2</biblScope>
                  <biblScope unit="pp">370</biblScope>
                  <date type="datePub">2020</date>
                  <date type="dateEpub">2021-01-19</date>
                </imprint>
              </monogr>
              <idno type="doi">10.1016/j.bpj.2020.12.006</idno>
              <ref type="publisher">https://www.cell.com/biophysj/fulltext/S0006-3495(20)33208-2</ref>
            </biblStruct>
          </sourceDesc>
          <profileDesc>
            <langUsage>
              <language ident="en">English</language>
            </langUsage>
            <textClass>
              <classCode scheme="halDomain" n="phys.phys.phys-bio-ph">Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph]</classCode>
              <classCode scheme="halDomain" n="sdv.bbm.gtp">Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN]</classCode>
              <classCode scheme="halTypology" n="ART">Journal articles</classCode>
              <classCode scheme="halOldTypology" n="ART">Journal articles</classCode>
              <classCode scheme="halTreeTypology" n="ART">Journal articles</classCode>
            </textClass>
            <abstract xml:lang="en">
              <p>The chromosomal DNA of bacteria is folded into a compact body called the nucleoid, which is composed essentially of DNA (80%), RNA (10%), and a number of different proteins (10%). These nucleoid proteins act as regulators of gene expression and influence the organization of the nucleoid by bridging, bending, or wrapping the DNA. These so-called architectural properties of nucleoid proteins are still poorly understood. For example, the reason why certain proteins compact the DNA coil in certain environments but make instead the DNA more rigid in other environments is the matter of ongoing debates. Here, we address the question of the impact of the self-association of nucleoid proteins on their architectural properties and try to determine whether differences in self-association are sufficient to induce large changes in the organization of the DNA coil. More specifically, we developed two coarse-grained models of proteins, which interact identically with the DNA but self-associate differently by forming either clusters or filaments in the absence of the DNA. We showed through Brownian dynamics simulations that self-association of the proteins increases dramatically their ability to shape the DNA coil. Moreover, we observed that cluster-forming proteins compact significantly the DNA coil (similar to the DNA-bridging mode of H-NS proteins), whereas filament-forming proteins increase instead significantly the stiffness of the DNA chain (similar to the DNA-stiffening mode of H-NS proteins). This work consequently suggests that the knowledge of the DNA-binding properties of the proteins is in itself not sufficient to understand their architectural properties. Rather, their self-association properties must also be investigated in detail, because they might actually drive the formation of different DNA/protein complexes.</p>
            </abstract>
          </profileDesc>
        </biblFull>
      </listBibl>
    </body>
    <back>
      <listOrg type="structures">
        <org type="laboratory" xml:id="struct-1043294" status="VALID">
          <idno type="IdRef">035460849</idno>
          <idno type="ISNI">0000 0000 9272 9931</idno>
          <idno type="RNSR">201122569N</idno>
          <idno type="ROR">https://ror.org/023n9q531</idno>
          <orgName>Laboratoire Interdisciplinaire de Physique [Saint Martin d’Hères]</orgName>
          <orgName type="acronym">LIPhy</orgName>
          <date type="start">2020-01-01</date>
          <desc>
            <address>
              <addrLine>140 rue de la Physique38058 Grenoble cedex 9</addrLine>
              <country key="FR"/>
            </address>
            <ref type="url">https://www-liphy.ujf-grenoble.fr/</ref>
          </desc>
          <listRelation>
            <relation name="UMR5588" active="#struct-441569" type="direct"/>
            <relation active="#struct-1042703" type="direct"/>
          </listRelation>
        </org>
        <org type="regroupinstitution" xml:id="struct-441569" status="VALID">
          <idno type="IdRef">02636817X</idno>
          <idno type="ISNI">0000000122597504</idno>
          <idno type="ROR">https://ror.org/02feahw73</idno>
          <orgName>Centre National de la Recherche Scientifique</orgName>
          <orgName type="acronym">CNRS</orgName>
          <date type="start">1939-10-19</date>
          <desc>
            <address>
              <country key="FR"/>
            </address>
            <ref type="url">https://www.cnrs.fr/</ref>
          </desc>
        </org>
        <org type="regroupinstitution" xml:id="struct-1042703" status="VALID">
          <idno type="IdRef">240648315</idno>
          <idno type="ROR">https://ror.org/02rx3b187</idno>
          <orgName>Université Grenoble Alpes</orgName>
          <orgName type="acronym">UGA</orgName>
          <date type="start">2020-01-01</date>
          <desc>
            <address>
              <addrLine>Adresse CS 40700 - 38058 Grenoble cedex</addrLine>
              <country key="FR"/>
            </address>
            <ref type="url">http://www.univ-grenoble-alpes.fr</ref>
          </desc>
        </org>
      </listOrg>
    </back>
  </text>
</TEI>