Study on the ubiquitin ligase activity of rotavirus NSP1 protein / 中华实验和临床病毒学杂志
Chinese Journal of Experimental and Clinical Virology
; (6): 451-454, 2010.
Article
de Zh
| WPRIM
| ID: wpr-231221
Bibliothèque responsable:
WPRO
ABSTRACT
<p><b>OBJECTIVE</b>To confirm the activity of non structural protein 1 (NSP1) of Rotavirus (RV) as E3 ubiquitin ligase by experiments and to provide some clues for NSP1 on the pathogenic mechanisms and replication of RV.</p><p><b>METHODS</b>The whole gene and RING deleted mutation gene of NSP1 were coloned into pEGFPC1 expression plasmid, and transfected into human embryonic kidney (HEK) 293 FT cells with pBlue-Script-HA-Ubiquitin. The expression of proteins were proved by using con-focal microscope and western blotting. The ubiquination of proteins were detected by co-immunoprecite.</p><p><b>RESULTS</b>The cellular proteins of HEK293FT are ubiquinated by NSP1 protein and NSP1 protein was self-ubiquinated also.</p><p><b>CONCLUSIONS</b>It revealed that RV NSP1 had the activity of E3 ubiquitin ligase and it may play a role on the modulate mechanisms of ubiquination.</p>
Texte intégral:
1
Indice:
WPRIM
Sujet Principal:
Protéines virales non structurales
/
Rotavirus
/
Ubiquitin-protein ligases
/
Cellules HEK293
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Génétique
/
Métabolisme
Limites du sujet:
Humans
langue:
Zh
Texte intégral:
Chinese Journal of Experimental and Clinical Virology
Année:
2010
Type:
Article