Binding properties of the complex formed by the Arabidopsis TALE homeodomain proteins STM and BLH3 to DNA containing single and double target sites

Autores
Viola, Ivana Lorena; Gonzalez, Daniel Hector
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
We have analyzed the DNA-binding properties of the complex formed by the Arabidopsis TALE homeodomain (HD) proteins STM and BLH3 in comparison with those of the individual proteins. In vitro DNA-binding assays indicated that complex formation increases binding affinity for sequences carrying either a single target site or two such sites arranged in tandem. Complex formation is not correlated with the establishment of new detectable contacts as deduced from missing-nucleoside experiments. Increased binding was also observed when using BLH3 with a mutation that renders the HD unable to bind DNA, suggesting that only the STM functional HD is necessary for tight binding by the complex. Yeast one-hybrid assays using single or double target sites showed that the effect of complex formation is more dramatic for the double target site and that under these conditions competition for binding by the individual proteins is reduced. The results indicate that even if complex formation produces an increase in binding to DNA sequences containing either one or two target sites, the relative increase in binding produced after complex formation is dependent on the type of target sequence that is considered. This differential effect of complex formation on binding may have implications in the regulatory properties of these transcription factors within the cell.
Fil: Viola, Ivana Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
Fil: Gonzalez, Daniel Hector. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
Materia
ARABIDOPSIS THALIANA
BELL PROTEIN
COMPLEX FORMATION
DNA BINDING
KNOX PROTEIN
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/84792
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/84792
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Binding properties of the complex formed by the Arabidopsis TALE homeodomain proteins STM and BLH3 to DNA containing single and double target sitesViola, Ivana LorenaGonzalez, Daniel HectorARABIDOPSIS THALIANABELL PROTEINCOMPLEX FORMATIONDNA BINDINGKNOX PROTEINhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1We have analyzed the DNA-binding properties of the complex formed by the Arabidopsis TALE homeodomain (HD) proteins STM and BLH3 in comparison with those of the individual proteins. In vitro DNA-binding assays indicated that complex formation increases binding affinity for sequences carrying either a single target site or two such sites arranged in tandem. Complex formation is not correlated with the establishment of new detectable contacts as deduced from missing-nucleoside experiments. Increased binding was also observed when using BLH3 with a mutation that renders the HD unable to bind DNA, suggesting that only the STM functional HD is necessary for tight binding by the complex. Yeast one-hybrid assays using single or double target sites showed that the effect of complex formation is more dramatic for the double target site and that under these conditions competition for binding by the individual proteins is reduced. The results indicate that even if complex formation produces an increase in binding to DNA sequences containing either one or two target sites, the relative increase in binding produced after complex formation is dependent on the type of target sequence that is considered. This differential effect of complex formation on binding may have implications in the regulatory properties of these transcription factors within the cell.Fil: Viola, Ivana Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; ArgentinaFil: Gonzalez, Daniel Hector. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; ArgentinaElsevier France-editions Scientifiques Medicales Elsevier2009-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/84792Viola, Ivana Lorena; Gonzalez, Daniel Hector; Binding properties of the complex formed by the Arabidopsis TALE homeodomain proteins STM and BLH3 to DNA containing single and double target sites; Elsevier France-editions Scientifiques Medicales Elsevier; Biochimie; 91; 8; 8-2009; 974-9810300-9084CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.biochi.2009.04.021info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:20:52Zoai:ri.conicet.gov.ar:11336/84792instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 14:20:52.887CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Binding properties of the complex formed by the Arabidopsis TALE homeodomain proteins STM and BLH3 to DNA containing single and double target sites
title Binding properties of the complex formed by the Arabidopsis TALE homeodomain proteins STM and BLH3 to DNA containing single and double target sites
spellingShingle Binding properties of the complex formed by the Arabidopsis TALE homeodomain proteins STM and BLH3 to DNA containing single and double target sites
Viola, Ivana Lorena
ARABIDOPSIS THALIANA
BELL PROTEIN
COMPLEX FORMATION
DNA BINDING
KNOX PROTEIN
title_short Binding properties of the complex formed by the Arabidopsis TALE homeodomain proteins STM and BLH3 to DNA containing single and double target sites
title_full Binding properties of the complex formed by the Arabidopsis TALE homeodomain proteins STM and BLH3 to DNA containing single and double target sites
title_fullStr Binding properties of the complex formed by the Arabidopsis TALE homeodomain proteins STM and BLH3 to DNA containing single and double target sites
title_full_unstemmed Binding properties of the complex formed by the Arabidopsis TALE homeodomain proteins STM and BLH3 to DNA containing single and double target sites
title_sort Binding properties of the complex formed by the Arabidopsis TALE homeodomain proteins STM and BLH3 to DNA containing single and double target sites
dc.creator.none.fl_str_mv Viola, Ivana Lorena
Gonzalez, Daniel Hector
author Viola, Ivana Lorena
author_facet Viola, Ivana Lorena
Gonzalez, Daniel Hector
author_role author
author2 Gonzalez, Daniel Hector
author2_role author
dc.subject.none.fl_str_mv ARABIDOPSIS THALIANA
BELL PROTEIN
COMPLEX FORMATION
DNA BINDING
KNOX PROTEIN
topic ARABIDOPSIS THALIANA
BELL PROTEIN
COMPLEX FORMATION
DNA BINDING
KNOX PROTEIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv We have analyzed the DNA-binding properties of the complex formed by the Arabidopsis TALE homeodomain (HD) proteins STM and BLH3 in comparison with those of the individual proteins. In vitro DNA-binding assays indicated that complex formation increases binding affinity for sequences carrying either a single target site or two such sites arranged in tandem. Complex formation is not correlated with the establishment of new detectable contacts as deduced from missing-nucleoside experiments. Increased binding was also observed when using BLH3 with a mutation that renders the HD unable to bind DNA, suggesting that only the STM functional HD is necessary for tight binding by the complex. Yeast one-hybrid assays using single or double target sites showed that the effect of complex formation is more dramatic for the double target site and that under these conditions competition for binding by the individual proteins is reduced. The results indicate that even if complex formation produces an increase in binding to DNA sequences containing either one or two target sites, the relative increase in binding produced after complex formation is dependent on the type of target sequence that is considered. This differential effect of complex formation on binding may have implications in the regulatory properties of these transcription factors within the cell.
Fil: Viola, Ivana Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
Fil: Gonzalez, Daniel Hector. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
description We have analyzed the DNA-binding properties of the complex formed by the Arabidopsis TALE homeodomain (HD) proteins STM and BLH3 in comparison with those of the individual proteins. In vitro DNA-binding assays indicated that complex formation increases binding affinity for sequences carrying either a single target site or two such sites arranged in tandem. Complex formation is not correlated with the establishment of new detectable contacts as deduced from missing-nucleoside experiments. Increased binding was also observed when using BLH3 with a mutation that renders the HD unable to bind DNA, suggesting that only the STM functional HD is necessary for tight binding by the complex. Yeast one-hybrid assays using single or double target sites showed that the effect of complex formation is more dramatic for the double target site and that under these conditions competition for binding by the individual proteins is reduced. The results indicate that even if complex formation produces an increase in binding to DNA sequences containing either one or two target sites, the relative increase in binding produced after complex formation is dependent on the type of target sequence that is considered. This differential effect of complex formation on binding may have implications in the regulatory properties of these transcription factors within the cell.
publishDate 2009
dc.date.none.fl_str_mv 2009-08
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/84792
Viola, Ivana Lorena; Gonzalez, Daniel Hector; Binding properties of the complex formed by the Arabidopsis TALE homeodomain proteins STM and BLH3 to DNA containing single and double target sites; Elsevier France-editions Scientifiques Medicales Elsevier; Biochimie; 91; 8; 8-2009; 974-981
0300-9084
CONICET Digital
CONICET
url http://hdl.handle.net/11336/84792
identifier_str_mv Viola, Ivana Lorena; Gonzalez, Daniel Hector; Binding properties of the complex formed by the Arabidopsis TALE homeodomain proteins STM and BLH3 to DNA containing single and double target sites; Elsevier France-editions Scientifiques Medicales Elsevier; Biochimie; 91; 8; 8-2009; 974-981
0300-9084
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.biochi.2009.04.021
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier France-editions Scientifiques Medicales Elsevier
publisher.none.fl_str_mv Elsevier France-editions Scientifiques Medicales Elsevier
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.22299

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