Links to Exploration step
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Membrane anchoring domain of herpes simplex virus glycoprotein gB is sufficient for nuclear envelope localization.</title>
<author><name sortKey="Gilbert, R" sort="Gilbert, R" uniqKey="Gilbert R" first="R" last="Gilbert">R. Gilbert</name>
</author>
<author><name sortKey="Ghosh, K" sort="Ghosh, K" uniqKey="Ghosh K" first="K" last="Ghosh">K. Ghosh</name>
</author>
<author><name sortKey="Rasile, L" sort="Rasile, L" uniqKey="Rasile L" first="L" last="Rasile">L. Rasile</name>
</author>
<author><name sortKey="Ghosh, H P" sort="Ghosh, H P" uniqKey="Ghosh H" first="H P" last="Ghosh">H P Ghosh</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PMC</idno>
<idno type="pmid">8139012</idno>
<idno type="pmc">236703</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC236703</idno>
<idno type="RBID">PMC:236703</idno>
<date when="1994">1994</date>
<idno type="wicri:Area/Pmc/Corpus">000478</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000478</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Membrane anchoring domain of herpes simplex virus glycoprotein gB is sufficient for nuclear envelope localization.</title>
<author><name sortKey="Gilbert, R" sort="Gilbert, R" uniqKey="Gilbert R" first="R" last="Gilbert">R. Gilbert</name>
</author>
<author><name sortKey="Ghosh, K" sort="Ghosh, K" uniqKey="Ghosh K" first="K" last="Ghosh">K. Ghosh</name>
</author>
<author><name sortKey="Rasile, L" sort="Rasile, L" uniqKey="Rasile L" first="L" last="Rasile">L. Rasile</name>
</author>
<author><name sortKey="Ghosh, H P" sort="Ghosh, H P" uniqKey="Ghosh H" first="H P" last="Ghosh">H P Ghosh</name>
</author>
</analytic>
<series><title level="j">Journal of Virology</title>
<idno type="ISSN">0022-538X</idno>
<idno type="eISSN">1098-5514</idno>
<imprint><date when="1994">1994</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p>We have used the glycoprotein gB of herpes simplex virus type 1 (gB-1), which buds from the inner nuclear membrane, as a model protein to study localization of membrane proteins in the nuclear envelope. To determine whether specific domains of gB-1 glycoprotein are involved in localization in the nuclear envelope, we have used deletion mutants of gB-1 protein as well as chimeric proteins constructed by replacing the domains of the cell surface glycoprotein G of vesicular stomatitis virus with the corresponding domains of gB. Mutant and chimeric proteins expressed in COS cells were localized by immunoelectron microscopy. A chimeric protein (gB-G) containing the ectodomain of gB and the transmembrane and cytoplasmic domains of G did not localize in the nuclear envelope. When the ectodomain of G was fused to the transmembrane and cytoplasmic domains of gB, however, the resulting chimeric protein (G-gB) was localized in the nuclear envelope. Substitution of the transmembrane domain of G with the 69 hydrophobic amino acids containing the membrane anchoring domain of gB allowed the hybrid protein (G-tmgB) to be localized in the nuclear envelope, suggesting that residues 721 to 795 of gB can promote retention of proteins in the nuclear envelope. Deletion mutations in the hydrophobic region further showed that a transmembrane segment of 21 hydrophobic amino acids, residues 774 to 795 of gB, was sufficient for localization in the nuclear envelope. Since wild-type gB and the mutant and chimeric proteins that were localized in the nuclear envelope were also retained in the endoplasmic reticulum, the membrane spanning segment of gB could also influence retention in the endoplasmic reticulum.</p>
<sec sec-type="scanned-figures"><title>Images</title>
<fig id="F1"><graphic xlink:href="jvirol00013-0248-a" xlink:role="2274"></graphic>
</fig>
<fig id="F2"><graphic xlink:href="jvirol00013-0249-a" xlink:role="2275"></graphic>
</fig>
<fig id="F3"><graphic xlink:href="jvirol00013-0250-a" xlink:role="2276"></graphic>
</fig>
<fig id="F4"><graphic xlink:href="jvirol00013-0251-a" xlink:role="2277"></graphic>
</fig>
<fig id="F5"><graphic xlink:href="jvirol00013-0253-a" xlink:role="2279"></graphic>
</fig>
<fig id="F6"><graphic xlink:href="jvirol00013-0254-a" xlink:role="2280"></graphic>
</fig>
<fig id="F7"><graphic xlink:href="jvirol00013-0255-a" xlink:role="2281"></graphic>
</fig>
<fig id="F8"><graphic xlink:href="jvirol00013-0256-a" xlink:role="2282"></graphic>
</fig>
</sec>
</div>
</front>
</TEI>
<pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Virol</journal-id>
<journal-title>Journal of Virology</journal-title>
<issn pub-type="ppub">0022-538X</issn>
<issn pub-type="epub">1098-5514</issn>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">8139012</article-id>
<article-id pub-id-type="pmc">236703</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject>
</subj-group>
</article-categories>
<title-group><article-title>Membrane anchoring domain of herpes simplex virus glycoprotein gB is sufficient for nuclear envelope localization.</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Gilbert</surname>
<given-names>R</given-names>
</name>
</contrib>
<contrib contrib-type="author"><name><surname>Ghosh</surname>
<given-names>K</given-names>
</name>
</contrib>
<contrib contrib-type="author"><name><surname>Rasile</surname>
<given-names>L</given-names>
</name>
</contrib>
<contrib contrib-type="author"><name><surname>Ghosh</surname>
<given-names>H P</given-names>
</name>
</contrib>
</contrib-group>
<aff>Department of Biochemistry, McMaster University, Hamilton, Ontario, Canada.</aff>
<pub-date pub-type="ppub"><month>4</month>
<year>1994</year>
</pub-date>
<volume>68</volume>
<issue>4</issue>
<fpage>2272</fpage>
<lpage>2285</lpage>
<abstract><p>We have used the glycoprotein gB of herpes simplex virus type 1 (gB-1), which buds from the inner nuclear membrane, as a model protein to study localization of membrane proteins in the nuclear envelope. To determine whether specific domains of gB-1 glycoprotein are involved in localization in the nuclear envelope, we have used deletion mutants of gB-1 protein as well as chimeric proteins constructed by replacing the domains of the cell surface glycoprotein G of vesicular stomatitis virus with the corresponding domains of gB. Mutant and chimeric proteins expressed in COS cells were localized by immunoelectron microscopy. A chimeric protein (gB-G) containing the ectodomain of gB and the transmembrane and cytoplasmic domains of G did not localize in the nuclear envelope. When the ectodomain of G was fused to the transmembrane and cytoplasmic domains of gB, however, the resulting chimeric protein (G-gB) was localized in the nuclear envelope. Substitution of the transmembrane domain of G with the 69 hydrophobic amino acids containing the membrane anchoring domain of gB allowed the hybrid protein (G-tmgB) to be localized in the nuclear envelope, suggesting that residues 721 to 795 of gB can promote retention of proteins in the nuclear envelope. Deletion mutations in the hydrophobic region further showed that a transmembrane segment of 21 hydrophobic amino acids, residues 774 to 795 of gB, was sufficient for localization in the nuclear envelope. Since wild-type gB and the mutant and chimeric proteins that were localized in the nuclear envelope were also retained in the endoplasmic reticulum, the membrane spanning segment of gB could also influence retention in the endoplasmic reticulum.</p>
<sec sec-type="scanned-figures"><title>Images</title>
<fig id="F1"><graphic xlink:href="jvirol00013-0248-a" xlink:role="2274"></graphic>
</fig>
<fig id="F2"><graphic xlink:href="jvirol00013-0249-a" xlink:role="2275"></graphic>
</fig>
<fig id="F3"><graphic xlink:href="jvirol00013-0250-a" xlink:role="2276"></graphic>
</fig>
<fig id="F4"><graphic xlink:href="jvirol00013-0251-a" xlink:role="2277"></graphic>
</fig>
<fig id="F5"><graphic xlink:href="jvirol00013-0253-a" xlink:role="2279"></graphic>
</fig>
<fig id="F6"><graphic xlink:href="jvirol00013-0254-a" xlink:role="2280"></graphic>
</fig>
<fig id="F7"><graphic xlink:href="jvirol00013-0255-a" xlink:role="2281"></graphic>
</fig>
<fig id="F8"><graphic xlink:href="jvirol00013-0256-a" xlink:role="2282"></graphic>
</fig>
</sec>
</abstract>
</article-meta>
</front>
</pmc>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/CovidV2/Data/Pmc/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000478 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Pmc/Corpus/biblio.hfd -nk 000478 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Wicri/Sante |area= CovidV2 |flux= Pmc |étape= Corpus |type= RBID |clé= |texte= }}
![]() | This area was generated with Dilib version V0.6.33. | ![]() |