PoplarV1, Main, Exploration, bibRecord, 003A67

Tandem duplications of a degenerated GTP-binding domain at the origin of GTPase receptors Toc159 and thylakoidal SRP.

Identifieur interne : 003A67 ( Main/Exploration ); précédent : 003A66; suivant : 003A68

Tandem duplications of a degenerated GTP-binding domain at the origin of GTPase receptors Toc159 and thylakoidal SRP.

Auteurs : Jorge Hernández Torres [Colombie] ; M Nica Alexandra Arias Maldonado ; Jacques Chomilier

Source :

Biochemical and biophysical research communications [ 1090-2104 ] ; 2007.

RBID : pubmed:17950698

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Arabidopsis (genetics), Arabidopsis Proteins (genetics), GTP Phosphohydrolases (genetics), Genome, Plant (MeSH), Medicago truncatula (genetics), Membrane Proteins (genetics), Molecular Sequence Data (MeSH), Oryza (genetics), Peas (genetics), Populus (genetics), Protein Structure, Tertiary (MeSH), Protein Subunits (genetics), Sequence Homology, Amino Acid (MeSH), Signal Recognition Particle (genetics), Thylakoids (metabolism).
MESH :
- chemical , genetics : Arabidopsis Proteins, GTP Phosphohydrolases, Membrane Proteins, Protein Subunits, Signal Recognition Particle.
- genetics : Arabidopsis, Medicago truncatula, Oryza, Peas, Populus.
- metabolism : Thylakoids.
- Amino Acid Sequence, Genome, Plant, Molecular Sequence Data, Protein Structure, Tertiary, Sequence Homology, Amino Acid.

Abstract

The evolutionary origin of some nuclear encoded proteins that translocate proteins across the chloroplast envelope remains unknown. Therefore, sequences of GTPase proteins constituting the Arabidopsis thaliana translocon at the outer membrane of chloroplast (atToc) complexes were analyzed by means of HCA. In particular, atToc159 and related proteins (atToc132, atToc120, and atToc90) do not have proven homologues of prokaryotic or eukaryotic ancestry. We established that the three domains commonly referred to as A, G, and M originate from the GTPase G domain, tandemly repeated, and probably evolving toward an unstructured conformation in the case of the A domain. It resulted from this study a putative common ancestor for these proteins and a new domain definition, in particular the splitting of A into three domains (A1, A2, and A3), has been proposed. The family of Toc159, previously containing A. thaliana and Pisum sativum, has been extended to Medicago truncatula and Populus trichocarpa and it has been revised for Oryza sativa. They have also been compared to GTPase subunits involved in the cpSRP system. A distant homology has been revealed among Toc and cpSRP GTP-hydrolyzing proteins of A. thaliana, and repetitions of a GTPase domain were also found in cpSRP protein receptors, by means of HCA analysis.

DOI: 10.1016/j.bbrc.2007.10.006
PubMed: 17950698

Affiliations:

Colombie

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Le document en format XML

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<author><name sortKey="Hernandez Torres, Jorge" sort="Hernandez Torres, Jorge" uniqKey="Hernandez Torres J" first="Jorge" last="Hernández Torres">Jorge Hernández Torres</name>
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<author><name sortKey="Maldonado, M Nica Alexandra Arias" sort="Maldonado, M Nica Alexandra Arias" uniqKey="Maldonado M" first="M Nica Alexandra Arias" last="Maldonado">M Nica Alexandra Arias Maldonado</name>
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<term>Medicago truncatula (genetics)</term>
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<term>Molecular Sequence Data (MeSH)</term>
<term>Oryza (genetics)</term>
<term>Peas (genetics)</term>
<term>Populus (genetics)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
<term>Protein Subunits (genetics)</term>
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<term>Signal Recognition Particle (genetics)</term>
<term>Thylakoids (metabolism)</term>
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<term>Medicago truncatula (génétique)</term>
<term>Oryza (génétique)</term>
<term>Particule de reconnaissance du signal (génétique)</term>
<term>Pois (génétique)</term>
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<term>Protéines d'Arabidopsis (génétique)</term>
<term>Protéines membranaires (génétique)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Sous-unités de protéines (génétique)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Thylacoïdes (métabolisme)</term>
<term>dGTPases (génétique)</term>
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<front><div type="abstract" xml:lang="en">The evolutionary origin of some nuclear encoded proteins that translocate proteins across the chloroplast envelope remains unknown. Therefore, sequences of GTPase proteins constituting the Arabidopsis thaliana translocon at the outer membrane of chloroplast (atToc) complexes were analyzed by means of HCA. In particular, atToc159 and related proteins (atToc132, atToc120, and atToc90) do not have proven homologues of prokaryotic or eukaryotic ancestry. We established that the three domains commonly referred to as A, G, and M originate from the GTPase G domain, tandemly repeated, and probably evolving toward an unstructured conformation in the case of the A domain. It resulted from this study a putative common ancestor for these proteins and a new domain definition, in particular the splitting of A into three domains (A1, A2, and A3), has been proposed. The family of Toc159, previously containing A. thaliana and Pisum sativum, has been extended to Medicago truncatula and Populus trichocarpa and it has been revised for Oryza sativa. They have also been compared to GTPase subunits involved in the cpSRP system. A distant homology has been revealed among Toc and cpSRP GTP-hydrolyzing proteins of A. thaliana, and repetitions of a GTPase domain were also found in cpSRP protein receptors, by means of HCA analysis.</div>
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<Abstract><AbstractText>The evolutionary origin of some nuclear encoded proteins that translocate proteins across the chloroplast envelope remains unknown. Therefore, sequences of GTPase proteins constituting the Arabidopsis thaliana translocon at the outer membrane of chloroplast (atToc) complexes were analyzed by means of HCA. In particular, atToc159 and related proteins (atToc132, atToc120, and atToc90) do not have proven homologues of prokaryotic or eukaryotic ancestry. We established that the three domains commonly referred to as A, G, and M originate from the GTPase G domain, tandemly repeated, and probably evolving toward an unstructured conformation in the case of the A domain. It resulted from this study a putative common ancestor for these proteins and a new domain definition, in particular the splitting of A into three domains (A1, A2, and A3), has been proposed. The family of Toc159, previously containing A. thaliana and Pisum sativum, has been extended to Medicago truncatula and Populus trichocarpa and it has been revised for Oryza sativa. They have also been compared to GTPase subunits involved in the cpSRP system. A distant homology has been revealed among Toc and cpSRP GTP-hydrolyzing proteins of A. thaliana, and repetitions of a GTPase domain were also found in cpSRP protein receptors, by means of HCA analysis.</AbstractText>
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Tandem duplications of a degenerated GTP-binding domain at the origin of GTPase receptors Toc159 and thylakoidal SRP.

Tandem duplications of a degenerated GTP-binding domain at the origin of GTPase receptors Toc159 and thylakoidal SRP.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

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