Host cell factors stimulate HIV-1 transcription by antagonizing substrate-binding function of Siah1 ubiquitin ligase to stabilize transcription elongation factor ELL2.


Journal

Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011

Informations de publication

Date de publication:
27 07 2020
Historique:
accepted: 19 05 2020
revised: 12 05 2020
received: 26 11 2019
pubmed: 2 6 2020
medline: 17 9 2020
entrez: 2 6 2020
Statut: ppublish

Résumé

The Siah1 and Siah2 ubiquitin ligases are implicated in diverse biological processes ranging from cellular stress responses, signaling to transcriptional regulation. A key substrate of Siah1 is ELL2, which undergoes proteolysis upon polyubiquitination. ELL2 stimulates transcriptional elongation and is a subunit of the Super Elongation Complex (SEC) essential for HIV-1 transactivation. Previously, multiple transcriptional and post-translational mechanisms are reported to control Siah's expression and activity. Here we show that the activity of Siah1/2 can also be suppressed by host cell factor 1 (HCF1), and the hitherto poorly characterized HCF2, which themselves are not degraded but can bind and block the substrate-binding domain (SBD) of Siah1/2 to prevent their autoubiquitination and trans-ubiquitination of downstream targets including ELL2. This effect stabilizes ELL2 and enhances the ELL2-SEC formation for robust HIV-1 transactivation. Thus, our study not only identifies HCF1/2 as novel activators of HIV-1 transcription through inhibiting Siah1 to stabilize ELL2, but also reveals the SBD of Siah1/2 as a previously unrecognized new target for HCF1/2 to exert this inhibition.

Identifiants

pubmed: 32479599
pii: 5849913
doi: 10.1093/nar/gkaa461
pmc: PMC7367184
doi:

Substances chimiques

ELL2 protein, human 0
Host Cell Factor C1 0
Nuclear Proteins 0
Transcriptional Elongation Factors 0
tat Gene Products, Human Immunodeficiency Virus 0
Ubiquitin-Protein Ligases EC 2.3.2.27
seven in absentia proteins EC 2.3.2.27

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

7321-7332

Informations de copyright

© The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.

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Auteurs

Jun Wu (J)

Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.

Yuhua Xue (Y)

School of Pharmaceutical Sciences, Xiamen University, Xiamen, Fujian 361005, China.

Xiang Gao (X)

School of Pharmaceutical Sciences, Xiamen University, Xiamen, Fujian 361005, China.

Qiang Zhou (Q)

Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.

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Classifications MeSH