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Conserved structural motifs at the C-Terminus of baculovirus protein IE0 are important for its functions in transactivation and supporting hr5-mediated DNA replication
Year:
2012
Source of publication :
Viruses
Authors :
Chejanovsky, Nor
;
.
Volume :
4
Co-Authors:
Luria, N., Entomology Department, Institute of Plant Protection, The Volcani Center, POB 6, Bet Dagan 50250, Israel
Lu, L., Key Laboratory of Exploration and Utilization of Aquatic Genetic Resources (Ministry of Education), College of Fisheries and Life Science, Shanghai Ocean University, Shanghai 201306, China
Chejanovsky, N., Entomology Department, Institute of Plant Protection, The Volcani Center, POB 6, Bet Dagan 50250, Israel
Facilitators :
From page:
761
To page:
776
(
Total pages:
16
)
Abstract:
IE0 and IE1 are transactivator proteins of the most studied baculovirus, the Autographa californica multiple nucleopolyhedrovirus (AcMNPV). IE0 is a 72.6 kDa protein identical to IE1 with the exception of its 54 N-terminal amino acid residues. To gain some insight about important structural motifs of IE0, we expressed the protein and C-terminal mutants of it under the control of the Drosophila heat shock promoter and studied the transactivation and replication functions of the transiently expressed proteins. IE0 was able to promote replication of a plasmid bearing the hr5 origin of replication of AcMNPV in transient transfections with a battery of eight plasmids expressing the AcMNPV genes dnapol, helicase, lef-1, lef-2, lef-3, p35, ie-2 and lef-7. IE0 transactivated expression of the baculovirus 39K promoter. Both functions of replication and transactivation were lost after introduction of selected mutations at the basic domain II and helix-loop-helix conserved structural motifs in the C-terminus of the protein. These IE0 mutants were unable to translocate to the cell nucleus. Our results point out the important role of some structural conserved motifs to the proper functioning of IE0. © 2012 by the authors; licensee MDPI, Basel, Switzerland.
Note:
Related Files :
Animals
carboxy terminal sequence
Gene
gene expression
lef 3 gene
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More details
DOI :
10.3390/v4050761
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
24126
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:05
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Scientific Publication
Conserved structural motifs at the C-Terminus of baculovirus protein IE0 are important for its functions in transactivation and supporting hr5-mediated DNA replication
4
Luria, N., Entomology Department, Institute of Plant Protection, The Volcani Center, POB 6, Bet Dagan 50250, Israel
Lu, L., Key Laboratory of Exploration and Utilization of Aquatic Genetic Resources (Ministry of Education), College of Fisheries and Life Science, Shanghai Ocean University, Shanghai 201306, China
Chejanovsky, N., Entomology Department, Institute of Plant Protection, The Volcani Center, POB 6, Bet Dagan 50250, Israel
Conserved structural motifs at the C-Terminus of baculovirus protein IE0 are important for its functions in transactivation and supporting hr5-mediated DNA replication
IE0 and IE1 are transactivator proteins of the most studied baculovirus, the Autographa californica multiple nucleopolyhedrovirus (AcMNPV). IE0 is a 72.6 kDa protein identical to IE1 with the exception of its 54 N-terminal amino acid residues. To gain some insight about important structural motifs of IE0, we expressed the protein and C-terminal mutants of it under the control of the Drosophila heat shock promoter and studied the transactivation and replication functions of the transiently expressed proteins. IE0 was able to promote replication of a plasmid bearing the hr5 origin of replication of AcMNPV in transient transfections with a battery of eight plasmids expressing the AcMNPV genes dnapol, helicase, lef-1, lef-2, lef-3, p35, ie-2 and lef-7. IE0 transactivated expression of the baculovirus 39K promoter. Both functions of replication and transactivation were lost after introduction of selected mutations at the basic domain II and helix-loop-helix conserved structural motifs in the C-terminus of the protein. These IE0 mutants were unable to translocate to the cell nucleus. Our results point out the important role of some structural conserved motifs to the proper functioning of IE0. © 2012 by the authors; licensee MDPI, Basel, Switzerland.
Scientific Publication
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