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Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines
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Zeitschriftentitel: | Genes & Development |
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Personen und Körperschaften: | , , , , |
In: | Genes & Development, 18, 2004, 23, S. 2867-2872 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Cold Spring Harbor Laboratory
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Schlagwörter: |
author_facet |
Yu, Yunkai Xiao, Zuoxiang Ehrlich, Elana S. Yu, Xianghui Yu, Xiao-Fang Yu, Yunkai Xiao, Zuoxiang Ehrlich, Elana S. Yu, Xianghui Yu, Xiao-Fang |
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author |
Yu, Yunkai Xiao, Zuoxiang Ehrlich, Elana S. Yu, Xianghui Yu, Xiao-Fang |
spellingShingle |
Yu, Yunkai Xiao, Zuoxiang Ehrlich, Elana S. Yu, Xianghui Yu, Xiao-Fang Genes & Development Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines Developmental Biology Genetics |
author_sort |
yu, yunkai |
spelling |
Yu, Yunkai Xiao, Zuoxiang Ehrlich, Elana S. Yu, Xianghui Yu, Xiao-Fang 0890-9369 1549-5477 Cold Spring Harbor Laboratory Developmental Biology Genetics http://dx.doi.org/10.1101/gad.1250204 <jats:p>APOBEC3G, which induces hypermutations in newly synthesized viral DNA, is suppressed by HIV-1 Vif, acting through Cul5-ElonginB-ElonginC E3 ubiquitin ligase. We have now characterized a novel SOCS box in HIV-1 Vif that mediates its interaction with ElonginC. In this SOCS box, alanine replaces the consensus cysteine in the previously identified SOCS box. This new motif was necessary but insufficient for interaction with Cul5-ElonginB-ElonginC, as two highly conserved Cys residues outside the SOCS box were required to interact with Cul5 but not ElonginC. Therefore, selective assembly with Cul5 versus Cul2 E3 may require protein interfaces besides the SOCS-box-ElonginC interaction.</jats:p> Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines Genes & Development |
doi_str_mv |
10.1101/gad.1250204 |
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Online Free |
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Biologie |
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ElectronicArticle |
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Cold Spring Harbor Laboratory, 2004 |
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Cold Spring Harbor Laboratory, 2004 |
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0890-9369 1549-5477 |
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0890-9369 1549-5477 |
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English |
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Cold Spring Harbor Laboratory (CrossRef) |
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2004 |
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Cold Spring Harbor Laboratory |
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Genes & Development |
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title |
Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines |
title_unstemmed |
Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines |
title_full |
Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines |
title_fullStr |
Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines |
title_full_unstemmed |
Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines |
title_short |
Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines |
title_sort |
selective assembly of hiv-1 vif-cul5-elonginb-elonginc e3 ubiquitin ligase complex through a novel socs box and upstream cysteines |
topic |
Developmental Biology Genetics |
url |
http://dx.doi.org/10.1101/gad.1250204 |
publishDate |
2004 |
physical |
2867-2872 |
description |
<jats:p>APOBEC3G, which induces hypermutations in newly synthesized viral DNA, is suppressed by HIV-1 Vif, acting through Cul5-ElonginB-ElonginC E3 ubiquitin ligase. We have now characterized a novel SOCS box in HIV-1 Vif that mediates its interaction with ElonginC. In this SOCS box, alanine replaces the consensus cysteine in the previously identified SOCS box. This new motif was necessary but insufficient for interaction with Cul5-ElonginB-ElonginC, as two highly conserved Cys residues outside the SOCS box were required to interact with Cul5 but not ElonginC. Therefore, selective assembly with Cul5 versus Cul2 E3 may require protein interfaces besides the SOCS-box-ElonginC interaction.</jats:p> |
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author | Yu, Yunkai, Xiao, Zuoxiang, Ehrlich, Elana S., Yu, Xianghui, Yu, Xiao-Fang |
author_facet | Yu, Yunkai, Xiao, Zuoxiang, Ehrlich, Elana S., Yu, Xianghui, Yu, Xiao-Fang, Yu, Yunkai, Xiao, Zuoxiang, Ehrlich, Elana S., Yu, Xianghui, Yu, Xiao-Fang |
author_sort | yu, yunkai |
container_issue | 23 |
container_start_page | 2867 |
container_title | Genes & Development |
container_volume | 18 |
description | <jats:p>APOBEC3G, which induces hypermutations in newly synthesized viral DNA, is suppressed by HIV-1 Vif, acting through Cul5-ElonginB-ElonginC E3 ubiquitin ligase. We have now characterized a novel SOCS box in HIV-1 Vif that mediates its interaction with ElonginC. In this SOCS box, alanine replaces the consensus cysteine in the previously identified SOCS box. This new motif was necessary but insufficient for interaction with Cul5-ElonginB-ElonginC, as two highly conserved Cys residues outside the SOCS box were required to interact with Cul5 but not ElonginC. Therefore, selective assembly with Cul5 versus Cul2 E3 may require protein interfaces besides the SOCS-box-ElonginC interaction.</jats:p> |
doi_str_mv | 10.1101/gad.1250204 |
facet_avail | Online, Free |
finc_class_facet | Biologie |
format | ElectronicArticle |
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imprint | Cold Spring Harbor Laboratory, 2004 |
imprint_str_mv | Cold Spring Harbor Laboratory, 2004 |
institution | DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4 |
issn | 0890-9369, 1549-5477 |
issn_str_mv | 0890-9369, 1549-5477 |
language | English |
last_indexed | 2024-03-01T18:07:26.188Z |
match_str | yu2004selectiveassemblyofhiv1vifcul5elonginbelongince3ubiquitinligasecomplexthroughanovelsocsboxandupstreamcysteines |
mega_collection | Cold Spring Harbor Laboratory (CrossRef) |
physical | 2867-2872 |
publishDate | 2004 |
publishDateSort | 2004 |
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series | Genes & Development |
source_id | 49 |
spelling | Yu, Yunkai Xiao, Zuoxiang Ehrlich, Elana S. Yu, Xianghui Yu, Xiao-Fang 0890-9369 1549-5477 Cold Spring Harbor Laboratory Developmental Biology Genetics http://dx.doi.org/10.1101/gad.1250204 <jats:p>APOBEC3G, which induces hypermutations in newly synthesized viral DNA, is suppressed by HIV-1 Vif, acting through Cul5-ElonginB-ElonginC E3 ubiquitin ligase. We have now characterized a novel SOCS box in HIV-1 Vif that mediates its interaction with ElonginC. In this SOCS box, alanine replaces the consensus cysteine in the previously identified SOCS box. This new motif was necessary but insufficient for interaction with Cul5-ElonginB-ElonginC, as two highly conserved Cys residues outside the SOCS box were required to interact with Cul5 but not ElonginC. Therefore, selective assembly with Cul5 versus Cul2 E3 may require protein interfaces besides the SOCS-box-ElonginC interaction.</jats:p> Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines Genes & Development |
spellingShingle | Yu, Yunkai, Xiao, Zuoxiang, Ehrlich, Elana S., Yu, Xianghui, Yu, Xiao-Fang, Genes & Development, Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines, Developmental Biology, Genetics |
title | Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines |
title_full | Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines |
title_fullStr | Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines |
title_full_unstemmed | Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines |
title_short | Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines |
title_sort | selective assembly of hiv-1 vif-cul5-elonginb-elonginc e3 ubiquitin ligase complex through a novel socs box and upstream cysteines |
title_unstemmed | Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines |
topic | Developmental Biology, Genetics |
url | http://dx.doi.org/10.1101/gad.1250204 |