Structural Requirements in the Membrane-Spanning Domain of the Paramyxovirus HN Protein for the Formation of a Stable Tetramer
Identifieur interne : 004130 ( Main/Exploration ); précédent : 004129; suivant : 004131Structural Requirements in the Membrane-Spanning Domain of the Paramyxovirus HN Protein for the Formation of a Stable Tetramer
Auteurs : Griffith D. Parks [États-Unis] ; Suzanne Pohlmann [États-Unis]Source :
- Virology [ 0042-6822 ] ; 1995.
Abstract
Abstract: The paramyxovirus hemagglutinin-neuraminidase (HN) is a type II homotetrameric integral membrane glycoprotein composed of a pair of disulfide-linked dimers that are held together by noncovalent bonds. To determine the role of the internal uncleaved signal-anchor (S/A) domain in stable tetramer formation, cDNA-derived HN mutants containing S/A substitutions were expressed in HeLa cells. The assembly into tetramers and ER-to-Golgi transport of the proteins were examined by sucrose gradient sedimentation and by endoglycosidase treatment. A leucine-scanning substitution analysis of the 19 residue S/A identified 2 polar residues (Ser 31 and Tyr 36) in the C-terminal end of the S/A that were important for the formation of a stable tetramer. While Ala, Cys, and Gly could functionally replace Set 31 in the formation of a stable tetramer, substitution with Leu or Phe resulted in mutants that were detected as disulfide-linked dimers. These results indicate that a small amino acid in position 31, rather than a specific residue per se, is an important assembly requirement in the S/A. In contrast to the size requirement for position 31, the conservative substitution of Tyr 36 with Phe produced an HN mutant that sedimented as a mixture of dimers, tetramers, and higher order oligomers, suggesting that proper assembly requires a Tyr in this position. The S/A mutants that were detected as disulfide-linked dimers showed only a slight reduction in ERto-Golgi transport (∼50% of WT), consistent with the proposal that the S/A substitutions had affected tetramer stability and not the formation of a transport-competent oligomer. These data indicate that there are different structural requirements for two positions in the C-terminal region of the HN S/A for the assembly of a stable tetramer.
Url:
DOI: 10.1006/viro.1995.1569
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: 001791
- to stream Istex, to step Curation: 001791
- to stream Istex, to step Checkpoint: 001821
- to stream Main, to step Merge: 004191
- to stream Main, to step Curation: 004130
Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structural Requirements in the Membrane-Spanning Domain of the Paramyxovirus HN Protein for the Formation of a Stable Tetramer</title>
<author><name sortKey="Parks, Griffith D" sort="Parks, Griffith D" uniqKey="Parks G" first="Griffith D." last="Parks">Griffith D. Parks</name>
</author>
<author><name sortKey="Pohlmann, Suzanne" sort="Pohlmann, Suzanne" uniqKey="Pohlmann S" first="Suzanne" last="Pohlmann">Suzanne Pohlmann</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">ISTEX</idno>
<idno type="RBID">ISTEX:A54AEB9022F2EA309E38F62A61937FA180E2353D</idno>
<date when="1995" year="1995">1995</date>
<idno type="doi">10.1006/viro.1995.1569</idno>
<idno type="url">https://api.istex.fr/ark:/67375/6H6-HPKM6N34-X/fulltext.pdf</idno>
<idno type="wicri:Area/Istex/Corpus">001791</idno>
<idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001791</idno>
<idno type="wicri:Area/Istex/Curation">001791</idno>
<idno type="wicri:Area/Istex/Checkpoint">001821</idno>
<idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">001821</idno>
<idno type="wicri:doubleKey">0042-6822:1995:Parks G:structural:requirements:in</idno>
<idno type="wicri:Area/Main/Merge">004191</idno>
<idno type="wicri:Area/Main/Curation">004130</idno>
<idno type="wicri:Area/Main/Exploration">004130</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Structural Requirements in the Membrane-Spanning Domain of the Paramyxovirus HN Protein for the Formation of a Stable Tetramer</title>
<author><name sortKey="Parks, Griffith D" sort="Parks, Griffith D" uniqKey="Parks G" first="Griffith D." last="Parks">Griffith D. Parks</name>
<affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Caroline du Nord</region>
</placeName>
<wicri:cityArea>Department of Microbiology and Immunology, Bowman Gray School of Medicine, and Department of Biology, Wake Forest University, Winston-Salem</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Pohlmann, Suzanne" sort="Pohlmann, Suzanne" uniqKey="Pohlmann S" first="Suzanne" last="Pohlmann">Suzanne Pohlmann</name>
<affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Caroline du Nord</region>
</placeName>
<wicri:cityArea>Department of Microbiology and Immunology, Bowman Gray School of Medicine, and Department of Biology, Wake Forest University, Winston-Salem</wicri:cityArea>
</affiliation>
</author>
</analytic>
<monogr></monogr>
<series><title level="j">Virology</title>
<title level="j" type="abbrev">YVIRO</title>
<idno type="ISSN">0042-6822</idno>
<imprint><publisher>ELSEVIER</publisher>
<date type="published" when="1995">1995</date>
<biblScope unit="volume">213</biblScope>
<biblScope unit="issue">1</biblScope>
<biblScope unit="page" from="263">263</biblScope>
<biblScope unit="page" to="270">270</biblScope>
</imprint>
<idno type="ISSN">0042-6822</idno>
</series>
</biblStruct>
</sourceDesc>
<seriesStmt><idno type="ISSN">0042-6822</idno>
</seriesStmt>
</fileDesc>
<profileDesc><textClass></textClass>
<langUsage><language ident="en">en</language>
</langUsage>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Abstract: The paramyxovirus hemagglutinin-neuraminidase (HN) is a type II homotetrameric integral membrane glycoprotein composed of a pair of disulfide-linked dimers that are held together by noncovalent bonds. To determine the role of the internal uncleaved signal-anchor (S/A) domain in stable tetramer formation, cDNA-derived HN mutants containing S/A substitutions were expressed in HeLa cells. The assembly into tetramers and ER-to-Golgi transport of the proteins were examined by sucrose gradient sedimentation and by endoglycosidase treatment. A leucine-scanning substitution analysis of the 19 residue S/A identified 2 polar residues (Ser 31 and Tyr 36) in the C-terminal end of the S/A that were important for the formation of a stable tetramer. While Ala, Cys, and Gly could functionally replace Set 31 in the formation of a stable tetramer, substitution with Leu or Phe resulted in mutants that were detected as disulfide-linked dimers. These results indicate that a small amino acid in position 31, rather than a specific residue per se, is an important assembly requirement in the S/A. In contrast to the size requirement for position 31, the conservative substitution of Tyr 36 with Phe produced an HN mutant that sedimented as a mixture of dimers, tetramers, and higher order oligomers, suggesting that proper assembly requires a Tyr in this position. The S/A mutants that were detected as disulfide-linked dimers showed only a slight reduction in ERto-Golgi transport (∼50% of WT), consistent with the proposal that the S/A substitutions had affected tetramer stability and not the formation of a transport-competent oligomer. These data indicate that there are different structural requirements for two positions in the C-terminal region of the HN S/A for the assembly of a stable tetramer.</div>
</front>
</TEI>
<affiliations><list><country><li>États-Unis</li>
</country>
<region><li>Caroline du Nord</li>
</region>
</list>
<tree><country name="États-Unis"><region name="Caroline du Nord"><name sortKey="Parks, Griffith D" sort="Parks, Griffith D" uniqKey="Parks G" first="Griffith D." last="Parks">Griffith D. Parks</name>
</region>
<name sortKey="Pohlmann, Suzanne" sort="Pohlmann, Suzanne" uniqKey="Pohlmann S" first="Suzanne" last="Pohlmann">Suzanne Pohlmann</name>
</country>
</tree>
</affiliations>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 004130 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 004130 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= MersV1 |flux= Main |étape= Exploration |type= RBID |clé= ISTEX:A54AEB9022F2EA309E38F62A61937FA180E2353D |texte= Structural Requirements in the Membrane-Spanning Domain of the Paramyxovirus HN Protein for the Formation of a Stable Tetramer }}
This area was generated with Dilib version V0.6.33. |