Conserved homeodomain cysteines confer redox sensitivity and influence the DNA binding properties of plant class III HD-Zip proteins

Autores
Comelli, Raul Nicolas; Gonzalez, Daniel Hector
Año de publicación
2007
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The role of four cysteines present within the homeodomain of the homeodomain-leucine zipper (HD-Zip) class III protein Athb-9 has been studied. DNA binding by the Athb-9 HD-Zip domain was only observed after incubation in the presence of reducing agents or the thioredoxin system, suggesting that the protein is sensitive to redox conditions. A similar behavior was observed for proteins that show the same binding specificity of Athb-9 present in nuclear extracts. The use of single and double mutants indicated that two out of three of the cysteines at positions 23, 38 and 42 are required for redox sensitivity, while Cys58 is not involved. A role of Cys23 and Cys58 in determining the DNA binding efficiency and specificity, respectively, of the reduced Athb-9 HD-Zip domain was also evident from these studies. It can be postulated that redox conditions may modulate the function of Athb-9 in plant development. Sequence conservation suggests that the results can be extended to all HD-Zip III transcription factors.
Fil: Comelli, Raul Nicolas. Universidad Nacional 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
DNA BINDING
HOMEODOMAIN
PLANT TRANSCRIPTION FACTOR
REDOX REGULATION
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:11336/84799
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Conserved homeodomain cysteines confer redox sensitivity and influence the DNA binding properties of plant class III HD-Zip proteinsComelli, Raul NicolasGonzalez, Daniel HectorARABIDOPSIS THALIANADNA BINDINGHOMEODOMAINPLANT TRANSCRIPTION FACTORREDOX REGULATIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The role of four cysteines present within the homeodomain of the homeodomain-leucine zipper (HD-Zip) class III protein Athb-9 has been studied. DNA binding by the Athb-9 HD-Zip domain was only observed after incubation in the presence of reducing agents or the thioredoxin system, suggesting that the protein is sensitive to redox conditions. A similar behavior was observed for proteins that show the same binding specificity of Athb-9 present in nuclear extracts. The use of single and double mutants indicated that two out of three of the cysteines at positions 23, 38 and 42 are required for redox sensitivity, while Cys58 is not involved. A role of Cys23 and Cys58 in determining the DNA binding efficiency and specificity, respectively, of the reduced Athb-9 HD-Zip domain was also evident from these studies. It can be postulated that redox conditions may modulate the function of Athb-9 in plant development. Sequence conservation suggests that the results can be extended to all HD-Zip III transcription factors.Fil: Comelli, Raul Nicolas. Universidad Nacional 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 Science Inc2007-11info: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/11336/84799Comelli, Raul Nicolas; Gonzalez, Daniel Hector; Conserved homeodomain cysteines confer redox sensitivity and influence the DNA binding properties of plant class III HD-Zip proteins; Elsevier Science Inc; Archives of Biochemistry and Biophysics; 467; 1; 11-2007; 41-470003-9861CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.abb.2007.08.003info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:57:28Zoai:ri.conicet.gov.ar:11336/84799instacron: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:34982025-09-03 09:57:29.101CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Conserved homeodomain cysteines confer redox sensitivity and influence the DNA binding properties of plant class III HD-Zip proteins
title Conserved homeodomain cysteines confer redox sensitivity and influence the DNA binding properties of plant class III HD-Zip proteins
spellingShingle Conserved homeodomain cysteines confer redox sensitivity and influence the DNA binding properties of plant class III HD-Zip proteins
Comelli, Raul Nicolas
ARABIDOPSIS THALIANA
DNA BINDING
HOMEODOMAIN
PLANT TRANSCRIPTION FACTOR
REDOX REGULATION
title_short Conserved homeodomain cysteines confer redox sensitivity and influence the DNA binding properties of plant class III HD-Zip proteins
title_full Conserved homeodomain cysteines confer redox sensitivity and influence the DNA binding properties of plant class III HD-Zip proteins
title_fullStr Conserved homeodomain cysteines confer redox sensitivity and influence the DNA binding properties of plant class III HD-Zip proteins
title_full_unstemmed Conserved homeodomain cysteines confer redox sensitivity and influence the DNA binding properties of plant class III HD-Zip proteins
title_sort Conserved homeodomain cysteines confer redox sensitivity and influence the DNA binding properties of plant class III HD-Zip proteins
dc.creator.none.fl_str_mv Comelli, Raul Nicolas
Gonzalez, Daniel Hector
author Comelli, Raul Nicolas
author_facet Comelli, Raul Nicolas
Gonzalez, Daniel Hector
author_role author
author2 Gonzalez, Daniel Hector
author2_role author
dc.subject.none.fl_str_mv ARABIDOPSIS THALIANA
DNA BINDING
HOMEODOMAIN
PLANT TRANSCRIPTION FACTOR
REDOX REGULATION
topic ARABIDOPSIS THALIANA
DNA BINDING
HOMEODOMAIN
PLANT TRANSCRIPTION FACTOR
REDOX REGULATION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The role of four cysteines present within the homeodomain of the homeodomain-leucine zipper (HD-Zip) class III protein Athb-9 has been studied. DNA binding by the Athb-9 HD-Zip domain was only observed after incubation in the presence of reducing agents or the thioredoxin system, suggesting that the protein is sensitive to redox conditions. A similar behavior was observed for proteins that show the same binding specificity of Athb-9 present in nuclear extracts. The use of single and double mutants indicated that two out of three of the cysteines at positions 23, 38 and 42 are required for redox sensitivity, while Cys58 is not involved. A role of Cys23 and Cys58 in determining the DNA binding efficiency and specificity, respectively, of the reduced Athb-9 HD-Zip domain was also evident from these studies. It can be postulated that redox conditions may modulate the function of Athb-9 in plant development. Sequence conservation suggests that the results can be extended to all HD-Zip III transcription factors.
Fil: Comelli, Raul Nicolas. Universidad Nacional 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 The role of four cysteines present within the homeodomain of the homeodomain-leucine zipper (HD-Zip) class III protein Athb-9 has been studied. DNA binding by the Athb-9 HD-Zip domain was only observed after incubation in the presence of reducing agents or the thioredoxin system, suggesting that the protein is sensitive to redox conditions. A similar behavior was observed for proteins that show the same binding specificity of Athb-9 present in nuclear extracts. The use of single and double mutants indicated that two out of three of the cysteines at positions 23, 38 and 42 are required for redox sensitivity, while Cys58 is not involved. A role of Cys23 and Cys58 in determining the DNA binding efficiency and specificity, respectively, of the reduced Athb-9 HD-Zip domain was also evident from these studies. It can be postulated that redox conditions may modulate the function of Athb-9 in plant development. Sequence conservation suggests that the results can be extended to all HD-Zip III transcription factors.
publishDate 2007
dc.date.none.fl_str_mv 2007-11
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/11336/84799
Comelli, Raul Nicolas; Gonzalez, Daniel Hector; Conserved homeodomain cysteines confer redox sensitivity and influence the DNA binding properties of plant class III HD-Zip proteins; Elsevier Science Inc; Archives of Biochemistry and Biophysics; 467; 1; 11-2007; 41-47
0003-9861
CONICET Digital
CONICET
url http://hdl.handle.net/11336/84799
identifier_str_mv Comelli, Raul Nicolas; Gonzalez, Daniel Hector; Conserved homeodomain cysteines confer redox sensitivity and influence the DNA binding properties of plant class III HD-Zip proteins; Elsevier Science Inc; Archives of Biochemistry and Biophysics; 467; 1; 11-2007; 41-47
0003-9861
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.abb.2007.08.003
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 Science Inc
publisher.none.fl_str_mv Elsevier Science Inc
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 13.13397

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