Oligomerization Mediated by a Helix-Loop-Helix-Like Domain of Baculovirus IE1 Is Required for Early Promoter Transactivation

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Published inJournal of Virology Vol. 75; no. 13; pp. 6042 - 6051
Main Authors Olson, V A, Wetter, J A, Friesen, P D
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.07.2001
Subjects
AIE1 protein
Autographa californica MNPV
Binding Sites
DNA, Viral - metabolism
DNA-Binding Proteins
Helix-Loop-Helix Motifs
IE1 protein
Immediate-Early Proteins - chemistry
Immediate-Early Proteins - physiology
Nuclear polyhedrosis virus
Promoter Regions, Genetic
Trans-Activators - chemistry
Trans-Activators - physiology
Transcriptional Activation
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Abstract Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JVI .asm.org, visit: JVI       
AbstractList IE1 is a principal transcriptional regulator of Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV). Transactivation by IE1 is stimulated when early viral promoters are cis linked to homologous-region (hr) enhancer sequences of AcMNPV. This transcriptional enhancement is correlated with the binding of IE1 as a dimer to the 28-bp palindromic repeats comprising the hr enhancer. To define the role of homophilic interactions in IE1 transactivation, we have mapped the IE1 domains required for oligomerization. We report here that IE1 oligomerizes by a mechanism independent of enhancer binding, as demonstrated by in vitro pull-down assays using fusions of IE1 (582 residues) to the C terminus of glutathione S-transferase. In vivo oligomerization of IE1 was verified by immunoprecipitation of IE1 complexes from extracts of plasmid-transfected SF21 cells. Analyses of a series of site- directed IE1 insertion mutations indicated that a helix-loop-helix (HLH)-like domain extending from residue 543 to residue 568 is the primary determinant of oligomerization. Replacement of residues within the hydrophobic face of the putative dimerization domain disrupted IE1 homophilic interactions and caused loss of IE1 transactivation of hr-dependent promoters in plasmid transfection assays. Thus, oligomerization is required for IE1 transcriptional stimulation. HLH mutations also reduced IE1 stability and abrogated transactivation of non-hr-dependent promoters. These data support a model wherein IE1 oligomerizes prior to DNA binding to facilitate proper interaction with the symmetrical recognition sites within the hr enhancer and thereby promote the transcription of early viral genes.
Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JVI .asm.org, visit: JVI       
IE1 is a principal transcriptional regulator of Autographa californica multicapsid nucleopolyhedrovirus (Ac M NPV). Transactivation by IE1 is stimulated when early viral promoters are cis linked to homologous-region ( hr ) enhancer sequences of Ac M NPV. This transcriptional enhancement is correlated with the binding of IE1 as a dimer to the 28-bp palindromic repeats comprising the hr enhancer. To define the role of homophilic interactions in IE1 transactivation, we have mapped the IE1 domains required for oligomerization. We report here that IE1 oligomerizes by a mechanism independent of enhancer binding, as demonstrated by in vitro pull-down assays using fusions of IE1 (582 residues) to the C terminus of glutathione S -transferase. In vivo oligomerization of IE1 was verified by immunoprecipitation of IE1 complexes from extracts of plasmid-transfected SF21 cells. Analyses of a series of site-directed IE1 insertion mutations indicated that a helix-loop-helix (HLH)-like domain extending from residue 543 to residue 568 is the primary determinant of oligomerization. Replacement of residues within the hydrophobic face of the putative dimerization domain disrupted IE1 homophilic interactions and caused loss of IE1 transactivation of hr -dependent promoters in plasmid transfection assays. Thus, oligomerization is required for IE1 transcriptional stimulation. HLH mutations also reduced IE1 stability and abrogated transactivation of non- hr -dependent promoters. These data support a model wherein IE1 oligomerizes prior to DNA binding to facilitate proper interaction with the symmetrical recognition sites within the hr enhancer and thereby promote the transcription of early viral genes.
ABSTRACT IE1 is a principal transcriptional regulator of Autographa californica multicapsid nucleopolyhedrovirus (Ac M NPV). Transactivation by IE1 is stimulated when early viral promoters are cis linked to homologous-region ( hr ) enhancer sequences of Ac M NPV. This transcriptional enhancement is correlated with the binding of IE1 as a dimer to the 28-bp palindromic repeats comprising the hr enhancer. To define the role of homophilic interactions in IE1 transactivation, we have mapped the IE1 domains required for oligomerization. We report here that IE1 oligomerizes by a mechanism independent of enhancer binding, as demonstrated by in vitro pull-down assays using fusions of IE1 (582 residues) to the C terminus of glutathione S -transferase. In vivo oligomerization of IE1 was verified by immunoprecipitation of IE1 complexes from extracts of plasmid-transfected SF21 cells. Analyses of a series of site-directed IE1 insertion mutations indicated that a helix-loop-helix (HLH)-like domain extending from residue 543 to residue 568 is the primary determinant of oligomerization. Replacement of residues within the hydrophobic face of the putative dimerization domain disrupted IE1 homophilic interactions and caused loss of IE1 transactivation of hr -dependent promoters in plasmid transfection assays. Thus, oligomerization is required for IE1 transcriptional stimulation. HLH mutations also reduced IE1 stability and abrogated transactivation of non- hr -dependent promoters. These data support a model wherein IE1 oligomerizes prior to DNA binding to facilitate proper interaction with the symmetrical recognition sites within the hr enhancer and thereby promote the transcription of early viral genes.
Author Justin A. Wetter
Victoria A. Olson
Paul D. Friesen
AuthorAffiliation Institute for Molecular Virology and Department of Biochemistry, Graduate School and College of Agricultural and Life Sciences, University of Wisconsin—Madison, Madison, Wisconsin 53706
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Corresponding author. Mailing address: Institute for Molecular Virology, Bock Laboratories, University of Wisconsin—Madison, 1525 Linden Dr., Madison, WI 53706-1596. Phone: (608) 262-7774. Fax: (608) 262-7414. E-mail: pfriesen@facstaff.wisc.edu.
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IE1 is a principal transcriptional regulator of Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV). Transactivation by IE1 is stimulated when...
ABSTRACT IE1 is a principal transcriptional regulator of Autographa californica multicapsid nucleopolyhedrovirus (Ac M NPV). Transactivation by IE1 is...
IE1 is a principal transcriptional regulator of Autographa californica multicapsid nucleopolyhedrovirus (Ac M NPV). Transactivation by IE1 is stimulated when...
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SubjectTerms AIE1 protein
Autographa californica MNPV
Binding Sites
DNA, Viral - metabolism
DNA-Binding Proteins
Helix-Loop-Helix Motifs
IE1 protein
Immediate-Early Proteins - chemistry
Immediate-Early Proteins - physiology
Nuclear polyhedrosis virus
Promoter Regions, Genetic
Trans-Activators - chemistry
Trans-Activators - physiology
Transcriptional Activation
Title Oligomerization Mediated by a Helix-Loop-Helix-Like Domain of Baculovirus IE1 Is Required for Early Promoter Transactivation
URI http://jvi.asm.org/content/75/13/6042.abstract
https://www.ncbi.nlm.nih.gov/pubmed/11390606
https://search.proquest.com/docview/17909652
https://search.proquest.com/docview/70895361
https://pubmed.ncbi.nlm.nih.gov/PMC114320
Volume 75
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