Uncharacterized conserved motifs outside the HD-Zip domain in HD-Zip subfamily I transcription factors; a potential source of functional diversity

<p>Abstract</p> <p>Background</p> <p>Plant HD-Zip transcription factors are modular proteins in which a homeodomain is associated to a leucine zipper. Of the four subfamilies in which they are divided, the tested members from subfamily I bind <it>in vitro </it&...

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Main Authors: Cabello Julieta V, Capella Matías, Raineri Jesica, Arce Agustín L, Chan Raquel L
Format: Article
Language:English
Published: BMC 2011-03-01
Series:BMC Plant Biology
Online Access:http://www.biomedcentral.com/1471-2229/11/42
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spelling doaj-167fe67d20c1472abb8266def4f5ed242020-11-25T00:20:59ZengBMCBMC Plant Biology1471-22292011-03-011114210.1186/1471-2229-11-42Uncharacterized conserved motifs outside the HD-Zip domain in HD-Zip subfamily I transcription factors; a potential source of functional diversityCabello Julieta VCapella MatíasRaineri JesicaArce Agustín LChan Raquel L<p>Abstract</p> <p>Background</p> <p>Plant HD-Zip transcription factors are modular proteins in which a homeodomain is associated to a leucine zipper. Of the four subfamilies in which they are divided, the tested members from subfamily I bind <it>in vitro </it>the same pseudopalindromic sequence CAAT(A/T)ATTG and among them, several exhibit similar expression patterns. However, most experiments in which HD-Zip I proteins were over or ectopically expressed under the control of the constitutive promoter 35S CaMV resulted in transgenic plants with clearly different phenotypes. Aiming to elucidate the structural mechanisms underlying such observation and taking advantage of the increasing information in databases of sequences from diverse plant species, an <it>in silico </it>analysis was performed. In addition, some of the results were also experimentally supported.</p> <p>Results</p> <p>A phylogenetic tree of 178 HD-Zip I proteins together with the sequence conservation presented outside the HD-Zip domains allowed the distinction of six groups of proteins. A motif-discovery approach enabled the recognition of an activation domain in the carboxy-terminal regions (CTRs) and some putative regulatory mechanisms acting in the amino-terminal regions (NTRs) and CTRs involving sumoylation and phosphorylation. A yeast one-hybrid experiment demonstrated that the activation activity of ATHB1, a member of one of the groups, is located in its CTR. Chimerical constructs were performed combining the HD-Zip domain of one member with the CTR of another and transgenic plants were obtained with these constructs. The phenotype of the chimerical transgenic plants was similar to the observed in transgenic plants bearing the CTR of the donor protein, revealing the importance of this module inside the whole protein.</p> <p>Conclusions</p> <p>The bioinformatical results and the experiments conducted in yeast and transgenic plants strongly suggest that the previously poorly analyzed NTRs and CTRs of HD-Zip I proteins play an important role in their function, hence potentially constituting a major source of functional diversity among members of this subfamily.</p> http://www.biomedcentral.com/1471-2229/11/42
collection DOAJ
language English
format Article
sources DOAJ
author Cabello Julieta V
Capella Matías
Raineri Jesica
Arce Agustín L
Chan Raquel L
spellingShingle Cabello Julieta V
Capella Matías
Raineri Jesica
Arce Agustín L
Chan Raquel L
Uncharacterized conserved motifs outside the HD-Zip domain in HD-Zip subfamily I transcription factors; a potential source of functional diversity
BMC Plant Biology
author_facet Cabello Julieta V
Capella Matías
Raineri Jesica
Arce Agustín L
Chan Raquel L
author_sort Cabello Julieta V
title Uncharacterized conserved motifs outside the HD-Zip domain in HD-Zip subfamily I transcription factors; a potential source of functional diversity
title_short Uncharacterized conserved motifs outside the HD-Zip domain in HD-Zip subfamily I transcription factors; a potential source of functional diversity
title_full Uncharacterized conserved motifs outside the HD-Zip domain in HD-Zip subfamily I transcription factors; a potential source of functional diversity
title_fullStr Uncharacterized conserved motifs outside the HD-Zip domain in HD-Zip subfamily I transcription factors; a potential source of functional diversity
title_full_unstemmed Uncharacterized conserved motifs outside the HD-Zip domain in HD-Zip subfamily I transcription factors; a potential source of functional diversity
title_sort uncharacterized conserved motifs outside the hd-zip domain in hd-zip subfamily i transcription factors; a potential source of functional diversity
publisher BMC
series BMC Plant Biology
issn 1471-2229
publishDate 2011-03-01
description <p>Abstract</p> <p>Background</p> <p>Plant HD-Zip transcription factors are modular proteins in which a homeodomain is associated to a leucine zipper. Of the four subfamilies in which they are divided, the tested members from subfamily I bind <it>in vitro </it>the same pseudopalindromic sequence CAAT(A/T)ATTG and among them, several exhibit similar expression patterns. However, most experiments in which HD-Zip I proteins were over or ectopically expressed under the control of the constitutive promoter 35S CaMV resulted in transgenic plants with clearly different phenotypes. Aiming to elucidate the structural mechanisms underlying such observation and taking advantage of the increasing information in databases of sequences from diverse plant species, an <it>in silico </it>analysis was performed. In addition, some of the results were also experimentally supported.</p> <p>Results</p> <p>A phylogenetic tree of 178 HD-Zip I proteins together with the sequence conservation presented outside the HD-Zip domains allowed the distinction of six groups of proteins. A motif-discovery approach enabled the recognition of an activation domain in the carboxy-terminal regions (CTRs) and some putative regulatory mechanisms acting in the amino-terminal regions (NTRs) and CTRs involving sumoylation and phosphorylation. A yeast one-hybrid experiment demonstrated that the activation activity of ATHB1, a member of one of the groups, is located in its CTR. Chimerical constructs were performed combining the HD-Zip domain of one member with the CTR of another and transgenic plants were obtained with these constructs. The phenotype of the chimerical transgenic plants was similar to the observed in transgenic plants bearing the CTR of the donor protein, revealing the importance of this module inside the whole protein.</p> <p>Conclusions</p> <p>The bioinformatical results and the experiments conducted in yeast and transgenic plants strongly suggest that the previously poorly analyzed NTRs and CTRs of HD-Zip I proteins play an important role in their function, hence potentially constituting a major source of functional diversity among members of this subfamily.</p>
url http://www.biomedcentral.com/1471-2229/11/42
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