PoplarV1, Main, Exploration, bibRecord, 003A06

A novel family of plant DNA-binding proteins containing both HMG-box and AT-rich interaction domains.

Identifieur interne : 003A06 ( Main/Exploration ); précédent : 003A05; suivant : 003A07

A novel family of plant DNA-binding proteins containing both HMG-box and AT-rich interaction domains.

Auteurs : Frederik T. Hansen [Danemark] ; Claus K. Madsen ; Anne Mette Nordland ; Marion Grasser ; Thomas Merkle ; Klaus D. Grasser

Source :

Biochemistry [ 1520-4995 ] ; 2008.

RBID : pubmed:19053246

Descripteurs français

English descriptors

KwdEn :
- AT Rich Sequence (MeSH), Amino Acid Sequence (MeSH), Animals (MeSH), Arabidopsis Proteins (chemistry), Arabidopsis Proteins (genetics), Arabidopsis Proteins (metabolism), Bryopsida (chemistry), Bryopsida (metabolism), DNA, Plant (chemistry), DNA, Plant (metabolism), DNA-Binding Proteins (chemistry), DNA-Binding Proteins (genetics), DNA-Binding Proteins (metabolism), HMG-Box Domains (MeSH), Molecular Sequence Data (MeSH), Oryza (chemistry), Oryza (metabolism), Populus (chemistry), Populus (metabolism), Protein Binding (MeSH), Zea mays (chemistry), Zea mays (metabolism).
MESH :
- chemical , chemistry : Arabidopsis Proteins, DNA, Plant, DNA-Binding Proteins.
- chemical , genetics : Arabidopsis Proteins, DNA-Binding Proteins.
- chemical , metabolism : Arabidopsis Proteins, DNA, Plant, DNA-Binding Proteins.
- chemistry : Bryopsida, Oryza, Populus, Zea mays.
- metabolism : Bryopsida, Oryza, Populus, Zea mays.
- AT Rich Sequence, Amino Acid Sequence, Animals, HMG-Box Domains, Molecular Sequence Data, Protein Binding.

Abstract

The A/T-rich interaction domain (ARID) and the HMG-box domain represent DNA-interaction modules that are found in sequence-specific as well as nonsequence-specific DNA-binding proteins. Both domains are found in a variety of DNA-interacting proteins in a wide range of eukaryotic organisms. Proteins that contain both an ARID and an HMG-box domain, here termed ARID-HMG proteins, appear to be specific for plants. This protein family is conserved in higher plants (both mono- and dicot plants) as well as lower plants such as the moss Physcomitrella. Since ARID-HMG proteins have not been studied experimentally, we have examined here two family members from Arabidopsis. The genes encoding ARID-HMG1 and ARID-HMG2 are widely expressed in Arabidopsis but at different levels. Subcellular localization experiments studying ARID-HMG1 and ARID-HMG2 fused to GFP by fluorescence microscopy show that both proteins localize primarily to cell nuclei. Analyses of the DNA-binding properties using electrophoretic mobility shift assays revealed that mediated by the HMG-box domain, ARID-HMG1 binds structure specifically to DNA minicircles. Mediated by the ARID, the protein binds preferentially to A/T-rich DNA, when compared with G/C-rich DNA. Therefore, both DNA-binding domains contribute to the DNA interactions of ARID-HMG1. Accordingly, the protein combines DNA-binding properties characteristic of ARID and HMG-box proteins.

DOI: 10.1021/bi801772k
PubMed: 19053246

Affiliations:

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>AT Rich Sequence (MeSH)</term>
<term>Amino Acid Sequence (MeSH)</term>
<term>Animals (MeSH)</term>
<term>Arabidopsis Proteins (chemistry)</term>
<term>Arabidopsis Proteins (genetics)</term>
<term>Arabidopsis Proteins (metabolism)</term>
<term>Bryopsida (chemistry)</term>
<term>Bryopsida (metabolism)</term>
<term>DNA, Plant (chemistry)</term>
<term>DNA, Plant (metabolism)</term>
<term>DNA-Binding Proteins (chemistry)</term>
<term>DNA-Binding Proteins (genetics)</term>
<term>DNA-Binding Proteins (metabolism)</term>
<term>HMG-Box Domains (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Oryza (chemistry)</term>
<term>Oryza (metabolism)</term>
<term>Populus (chemistry)</term>
<term>Populus (metabolism)</term>
<term>Protein Binding (MeSH)</term>
<term>Zea mays (chemistry)</term>
<term>Zea mays (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>ADN des plantes (composition chimique)</term>
<term>ADN des plantes (métabolisme)</term>
<term>Animaux (MeSH)</term>
<term>Bryopsida (composition chimique)</term>
<term>Bryopsida (métabolisme)</term>
<term>Domaines à boîtes HMG (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Oryza (composition chimique)</term>
<term>Oryza (métabolisme)</term>
<term>Populus (composition chimique)</term>
<term>Populus (métabolisme)</term>
<term>Protéines d'Arabidopsis (composition chimique)</term>
<term>Protéines d'Arabidopsis (génétique)</term>
<term>Protéines d'Arabidopsis (métabolisme)</term>
<term>Protéines de liaison à l'ADN (composition chimique)</term>
<term>Protéines de liaison à l'ADN (génétique)</term>
<term>Protéines de liaison à l'ADN (métabolisme)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Séquence riche en AT (MeSH)</term>
<term>Zea mays (composition chimique)</term>
<term>Zea mays (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Arabidopsis Proteins</term>
<term>DNA, Plant</term>
<term>DNA-Binding Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Arabidopsis Proteins</term>
<term>DNA-Binding Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Arabidopsis Proteins</term>
<term>DNA, Plant</term>
<term>DNA-Binding Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Bryopsida</term>
<term>Oryza</term>
<term>Populus</term>
<term>Zea mays</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>ADN des plantes</term>
<term>Bryopsida</term>
<term>Oryza</term>
<term>Populus</term>
<term>Protéines d'Arabidopsis</term>
<term>Protéines de liaison à l'ADN</term>
<term>Zea mays</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines d'Arabidopsis</term>
<term>Protéines de liaison à l'ADN</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Bryopsida</term>
<term>Oryza</term>
<term>Populus</term>
<term>Zea mays</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ADN des plantes</term>
<term>Bryopsida</term>
<term>Oryza</term>
<term>Populus</term>
<term>Protéines d'Arabidopsis</term>
<term>Protéines de liaison à l'ADN</term>
<term>Zea mays</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>AT Rich Sequence</term>
<term>Amino Acid Sequence</term>
<term>Animals</term>
<term>HMG-Box Domains</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
</keywords>
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<term>Domaines à boîtes HMG</term>
<term>Données de séquences moléculaires</term>
<term>Liaison aux protéines</term>
<term>Séquence d'acides aminés</term>
<term>Séquence riche en AT</term>
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<front><div type="abstract" xml:lang="en">The A/T-rich interaction domain (ARID) and the HMG-box domain represent DNA-interaction modules that are found in sequence-specific as well as nonsequence-specific DNA-binding proteins. Both domains are found in a variety of DNA-interacting proteins in a wide range of eukaryotic organisms. Proteins that contain both an ARID and an HMG-box domain, here termed ARID-HMG proteins, appear to be specific for plants. This protein family is conserved in higher plants (both mono- and dicot plants) as well as lower plants such as the moss Physcomitrella. Since ARID-HMG proteins have not been studied experimentally, we have examined here two family members from Arabidopsis. The genes encoding ARID-HMG1 and ARID-HMG2 are widely expressed in Arabidopsis but at different levels. Subcellular localization experiments studying ARID-HMG1 and ARID-HMG2 fused to GFP by fluorescence microscopy show that both proteins localize primarily to cell nuclei. Analyses of the DNA-binding properties using electrophoretic mobility shift assays revealed that mediated by the HMG-box domain, ARID-HMG1 binds structure specifically to DNA minicircles. Mediated by the ARID, the protein binds preferentially to A/T-rich DNA, when compared with G/C-rich DNA. Therefore, both DNA-binding domains contribute to the DNA interactions of ARID-HMG1. Accordingly, the protein combines DNA-binding properties characteristic of ARID and HMG-box proteins.</div>
</front>
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<Abstract><AbstractText>The A/T-rich interaction domain (ARID) and the HMG-box domain represent DNA-interaction modules that are found in sequence-specific as well as nonsequence-specific DNA-binding proteins. Both domains are found in a variety of DNA-interacting proteins in a wide range of eukaryotic organisms. Proteins that contain both an ARID and an HMG-box domain, here termed ARID-HMG proteins, appear to be specific for plants. This protein family is conserved in higher plants (both mono- and dicot plants) as well as lower plants such as the moss Physcomitrella. Since ARID-HMG proteins have not been studied experimentally, we have examined here two family members from Arabidopsis. The genes encoding ARID-HMG1 and ARID-HMG2 are widely expressed in Arabidopsis but at different levels. Subcellular localization experiments studying ARID-HMG1 and ARID-HMG2 fused to GFP by fluorescence microscopy show that both proteins localize primarily to cell nuclei. Analyses of the DNA-binding properties using electrophoretic mobility shift assays revealed that mediated by the HMG-box domain, ARID-HMG1 binds structure specifically to DNA minicircles. Mediated by the ARID, the protein binds preferentially to A/T-rich DNA, when compared with G/C-rich DNA. Therefore, both DNA-binding domains contribute to the DNA interactions of ARID-HMG1. Accordingly, the protein combines DNA-binding properties characteristic of ARID and HMG-box proteins.</AbstractText>
</Abstract>
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<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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A novel family of plant DNA-binding proteins containing both HMG-box and AT-rich interaction domains.

A novel family of plant DNA-binding proteins containing both HMG-box and AT-rich interaction domains.

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Abstract

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