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SUMOylated SNF2PH promotes variant surface glycoprotein expression in bloodstream trypanosomes
A. Saura, PA. Iribarren, D. Rojas-Barros, JM. Bart, D. López-Farfán, E. Andrés-León, I. Vidal-Cobo, C. Boehm, VE. Alvarez, MC. Field, M. Navarro,
Jazyk angličtina Země Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem
Grantová podpora
RTI2018-098834-B-I00
Ministerio de Ciencia, Innovación y Universidades - International
WTI 204697/Z/16/Z
Wellcome Trust - United Kingdom
PICT-2016-0465
Argentinian National Agency for Promotion of Scientific and Technological Research - International
NLK
Free Medical Journals
od 2000 do Před 1 rokem
Nature Open Access
od 2014-04-01
PubMed Central
od 2000
Europe PubMed Central
od 2000 do Před 1 rokem
Open Access Digital Library
od 2000-07-01
Medline Complete (EBSCOhost)
od 2000-07-01 do Před 1 rokem
Wiley Free Content
od 2000 do Před 1 rokem
Springer Nature OA/Free Journals
od 2014-04-01
PubMed
31693280
DOI
10.15252/embr.201948029
Knihovny.cz E-zdroje
- MeSH
- epigeneze genetická MeSH
- glykoproteiny genetika metabolismus MeSH
- protozoální proteiny genetika metabolismus MeSH
- restrukturace chromatinu MeSH
- RNA-polymerasa I metabolismus MeSH
- sumoylace * MeSH
- transkripční faktory genetika metabolismus MeSH
- Trypanosoma brucei brucei genetika metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
SUMOylation is a post-translational modification that positively regulates monoallelic expression of the trypanosome variant surface glycoprotein (VSG). The presence of a highly SUMOylated focus associated with the nuclear body, where the VSG gene is transcribed, further suggests an important role of SUMOylation in regulating VSG expression. Here, we show that SNF2PH, a SUMOylated plant homeodomain (PH)-transcription factor, is upregulated in the bloodstream form of the parasite and enriched at the active VSG telomere. SUMOylation promotes the recruitment of SNF2PH to the VSG promoter, where it is required to maintain RNA polymerase I and thus to regulate VSG transcript levels. Further, ectopic overexpression of SNF2PH in insect forms, but not of a mutant lacking the PH domain, induces the expression of bloodstream stage-specific surface proteins. These data suggest that SNF2PH SUMOylation positively regulates VSG monoallelic transcription, while the PH domain is required for the expression of bloodstream-specific surface proteins. Thus, SNF2PH functions as a positive activator, linking expression of infective form surface proteins and VSG regulation, thereby acting as a major regulator of pathogenicity.
IIB UNSAM Buenos Aires Argentina
Instituto de Parasitología y Biomedicina López Neyra CSIC Granada Spain
Citace poskytuje Crossref.org
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