Characterization of the protein product encoded by a splicing variant of the Marek's disease virus Eco-Q gene (Meq)

Virology
Q Peng, Y Shirazi

Abstract

In the present study, we report the characterization of a 212-amino-acid polypeptide encoded by a splicing variant of the Marek's disease virus Eco-Q gene (Meq). This protein, referred to as Meq-sp, contains the N-terminal 100 amino acids of Meq, which include part of Meq's DNA binding/dimerization domain, but lacks the transactivation domain of Meq. Thus, Meq-sp was examined for its ability to bind to DNA and act as a transactivator. Results indicated that while Meq and Meq-sp could both bind to the AP-1 binding site, the 110 C-terminal amino acid residues of Meq-sp lacked the ability to function as a transactivator when fused to the GAL4 (1-147) DNA binding motif. To investigate whether Meq-sp can interact with Meq or with c-jun, protein-protein and protein-DNA interactions in vitro were examined. Results showed that Meq-sp can associate with both Meq and c-jun and bind to the AP-1 site with a higher affinity as a heterodimer with c-jun. These results suggest that Meq-sp could compete with Meq for heterodimer formation with c-jun and dimer binding to DNA and possibly act as a transdominant negative regulator of Meq activity in vivo.

Citations

Aug 17, 2006·Journal of Virology·Joan BurnsideRobin W Morgan
Jul 31, 2002·Molecular Pathology : MP·E Le RouzicB Perbal
Aug 5, 2000·Research in Veterinary Science·K Venugopal
Mar 17, 2006·Nature Reviews. Microbiology·Nikolaus OsterriederSascha Trapp
Aug 17, 2018·The Journal of General Virology·Pratik Hemant KhedkarDusan Kunec
Aug 7, 2007·Cytogenetic and Genome Research·J Burnside, R W Morgan
Mar 22, 2007·The Journal of General Virology·Stephen J SpatzVenugopal Nair
Nov 26, 2020·The Journal of General Virology·Yifei LiaoBlanca Lupiani

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