Interaction of the BELL-like protein ATH1 with DNA: Role of homeodomain residue 54 in specifying the different binding properties of BELL and KNOX proteins

Autores
Viola, Ivana Lorena; Gonzalez, Daniel Hector
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
We have studied the interaction of the BELL-like Arabidopsis homeodomain protein ATH1 with DNA. Analysis of oligonucleotides selected by the ATH1 homeodomain from a random mixture suggests that ATH1 preferentially binds the sequence TGACAGGT. Single nucleotide replacements at positions 2 or 3 of this sequence abolish binding, while changes at position 4 are more tolerated. Changes outside this core differentially affect binding, depending on the position. Hydroxyl radical footprinting and missing nucleoside experiments showed that ATH1 interacts with a 7-bp region of the strand carrying the GAC core. On the other strand, protection was observed over a 7-bp region, comprising one additional nucleotide complementary to T in position 1. A comparative analysis of the binding preferences of the homeodomains of ATH1 and STM (a KNOX homeodomain protein) indicated that they bind similar sequences, but with differences in affinity and specificity. The decreased affinity displayed by the ATH1 homeodomain correlates with the presence of valine (instead of lysine as in STM) at position 54. This difference also explains the decreased and increased selectivities, respectively, at positions 4 and 5. Our results point to an essential role of residue 54 in determining the different binding properties of BELL and KNOX homeodomains.
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
BINDING-SITE SELECTION
DNA-BINDING SPECIFICITY
FOOTPRINTING
PLANT HOMEODOMAIN 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:11336/85783
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Interaction of the BELL-like protein ATH1 with DNA: Role of homeodomain residue 54 in specifying the different binding properties of BELL and KNOX proteinsViola, Ivana LorenaGonzalez, Daniel HectorBINDING-SITE SELECTIONDNA-BINDING SPECIFICITYFOOTPRINTINGPLANT HOMEODOMAIN PROTEINhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1We have studied the interaction of the BELL-like Arabidopsis homeodomain protein ATH1 with DNA. Analysis of oligonucleotides selected by the ATH1 homeodomain from a random mixture suggests that ATH1 preferentially binds the sequence TGACAGGT. Single nucleotide replacements at positions 2 or 3 of this sequence abolish binding, while changes at position 4 are more tolerated. Changes outside this core differentially affect binding, depending on the position. Hydroxyl radical footprinting and missing nucleoside experiments showed that ATH1 interacts with a 7-bp region of the strand carrying the GAC core. On the other strand, protection was observed over a 7-bp region, comprising one additional nucleotide complementary to T in position 1. A comparative analysis of the binding preferences of the homeodomains of ATH1 and STM (a KNOX homeodomain protein) indicated that they bind similar sequences, but with differences in affinity and specificity. The decreased affinity displayed by the ATH1 homeodomain correlates with the presence of valine (instead of lysine as in STM) at position 54. This difference also explains the decreased and increased selectivities, respectively, at positions 4 and 5. Our results point to an essential role of residue 54 in determining the different binding properties of BELL and KNOX homeodomains.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; ArgentinaDe Gruyter2006-01info: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/11336/85783Viola, Ivana Lorena; Gonzalez, Daniel Hector; Interaction of the BELL-like protein ATH1 with DNA: Role of homeodomain residue 54 in specifying the different binding properties of BELL and KNOX proteins; De Gruyter; Biological Chemistry; 387; 1; 1-2006; 31-401431-6730CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1515/BC.2006.006info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:18:42Zoai:ri.conicet.gov.ar:11336/85783instacron: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:34982025-09-10 13:18:42.731CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Interaction of the BELL-like protein ATH1 with DNA: Role of homeodomain residue 54 in specifying the different binding properties of BELL and KNOX proteins
title Interaction of the BELL-like protein ATH1 with DNA: Role of homeodomain residue 54 in specifying the different binding properties of BELL and KNOX proteins
spellingShingle Interaction of the BELL-like protein ATH1 with DNA: Role of homeodomain residue 54 in specifying the different binding properties of BELL and KNOX proteins
Viola, Ivana Lorena
BINDING-SITE SELECTION
DNA-BINDING SPECIFICITY
FOOTPRINTING
PLANT HOMEODOMAIN PROTEIN
title_short Interaction of the BELL-like protein ATH1 with DNA: Role of homeodomain residue 54 in specifying the different binding properties of BELL and KNOX proteins
title_full Interaction of the BELL-like protein ATH1 with DNA: Role of homeodomain residue 54 in specifying the different binding properties of BELL and KNOX proteins
title_fullStr Interaction of the BELL-like protein ATH1 with DNA: Role of homeodomain residue 54 in specifying the different binding properties of BELL and KNOX proteins
title_full_unstemmed Interaction of the BELL-like protein ATH1 with DNA: Role of homeodomain residue 54 in specifying the different binding properties of BELL and KNOX proteins
title_sort Interaction of the BELL-like protein ATH1 with DNA: Role of homeodomain residue 54 in specifying the different binding properties of BELL and KNOX proteins
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 BINDING-SITE SELECTION
DNA-BINDING SPECIFICITY
FOOTPRINTING
PLANT HOMEODOMAIN PROTEIN
topic BINDING-SITE SELECTION
DNA-BINDING SPECIFICITY
FOOTPRINTING
PLANT HOMEODOMAIN 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 studied the interaction of the BELL-like Arabidopsis homeodomain protein ATH1 with DNA. Analysis of oligonucleotides selected by the ATH1 homeodomain from a random mixture suggests that ATH1 preferentially binds the sequence TGACAGGT. Single nucleotide replacements at positions 2 or 3 of this sequence abolish binding, while changes at position 4 are more tolerated. Changes outside this core differentially affect binding, depending on the position. Hydroxyl radical footprinting and missing nucleoside experiments showed that ATH1 interacts with a 7-bp region of the strand carrying the GAC core. On the other strand, protection was observed over a 7-bp region, comprising one additional nucleotide complementary to T in position 1. A comparative analysis of the binding preferences of the homeodomains of ATH1 and STM (a KNOX homeodomain protein) indicated that they bind similar sequences, but with differences in affinity and specificity. The decreased affinity displayed by the ATH1 homeodomain correlates with the presence of valine (instead of lysine as in STM) at position 54. This difference also explains the decreased and increased selectivities, respectively, at positions 4 and 5. Our results point to an essential role of residue 54 in determining the different binding properties of BELL and KNOX homeodomains.
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 studied the interaction of the BELL-like Arabidopsis homeodomain protein ATH1 with DNA. Analysis of oligonucleotides selected by the ATH1 homeodomain from a random mixture suggests that ATH1 preferentially binds the sequence TGACAGGT. Single nucleotide replacements at positions 2 or 3 of this sequence abolish binding, while changes at position 4 are more tolerated. Changes outside this core differentially affect binding, depending on the position. Hydroxyl radical footprinting and missing nucleoside experiments showed that ATH1 interacts with a 7-bp region of the strand carrying the GAC core. On the other strand, protection was observed over a 7-bp region, comprising one additional nucleotide complementary to T in position 1. A comparative analysis of the binding preferences of the homeodomains of ATH1 and STM (a KNOX homeodomain protein) indicated that they bind similar sequences, but with differences in affinity and specificity. The decreased affinity displayed by the ATH1 homeodomain correlates with the presence of valine (instead of lysine as in STM) at position 54. This difference also explains the decreased and increased selectivities, respectively, at positions 4 and 5. Our results point to an essential role of residue 54 in determining the different binding properties of BELL and KNOX homeodomains.
publishDate 2006
dc.date.none.fl_str_mv 2006-01
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/11336/85783
Viola, Ivana Lorena; Gonzalez, Daniel Hector; Interaction of the BELL-like protein ATH1 with DNA: Role of homeodomain residue 54 in specifying the different binding properties of BELL and KNOX proteins; De Gruyter; Biological Chemistry; 387; 1; 1-2006; 31-40
1431-6730
CONICET Digital
CONICET
url http://hdl.handle.net/11336/85783
identifier_str_mv Viola, Ivana Lorena; Gonzalez, Daniel Hector; Interaction of the BELL-like protein ATH1 with DNA: Role of homeodomain residue 54 in specifying the different binding properties of BELL and KNOX proteins; De Gruyter; Biological Chemistry; 387; 1; 1-2006; 31-40
1431-6730
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1515/BC.2006.006
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 De Gruyter
publisher.none.fl_str_mv De Gruyter
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 12.993085

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