PoplarV1, Main, Exploration, bibRecord, 003D94

Identification of a new family of plant proteins loosely related to glutaredoxins with four CxxC motives.

Identifieur interne : 003D94 ( Main/Exploration ); précédent : 003D93; suivant : 003D95

Identification of a new family of plant proteins loosely related to glutaredoxins with four CxxC motives.

Auteurs : Nicolas Navrot [France] ; Eric Gelhaye ; Jean-Pierre Jacquot ; Nicolas Rouhier

Source :

Photosynthesis research [ 0166-8595 ] ; 2006.

RBID : pubmed:16915354

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Motifs (MeSH), Amino Acid Sequence (MeSH), Gene Expression Profiling (MeSH), Gene Expression Regulation, Plant (MeSH), Genome, Plant (MeSH), Glutaredoxins (MeSH), Molecular Sequence Data (MeSH), Multigene Family (MeSH), Oxidoreductases (chemistry), Oxidoreductases (classification), Phylogeny (MeSH), Plant Proteins (chemistry), Plant Proteins (classification), Plant Proteins (genetics), Populus (chemistry), Populus (genetics).
MESH :
- chemical , chemistry : Oxidoreductases, Plant Proteins.
- chemical , classification : Oxidoreductases, Plant Proteins.
- chemical , genetics : Plant Proteins.
- chemical : Glutaredoxins.
- chemistry : Populus.
- genetics : Populus.
- Amino Acid Motifs, Amino Acid Sequence, Gene Expression Profiling, Gene Expression Regulation, Plant, Genome, Plant, Molecular Sequence Data, Multigene Family, Phylogeny.

Abstract

The annotation of the recently released Populus trichocarpa genome, has allowed us to characterize extensively the multigenic families of the redoxin proteins. Proteins with two cysteines separated by two amino acids (CxxC motif) are often involved in redox reactions by promoting the formation, reduction or isomerization of disulfide bonds or by binding prosthetic groups or metals. We report here the presence of a new protein family in higher plants, constituted of 19 members in Populus trichocarpa, 15 in Arabidopsis thaliana and 17 in Oryza sativa. These proteins are almost specific to higher plants, with only two homologous genes found in mammals and arthropoda but none in other kingdoms. While these proteins were predicted as glutaredoxin-like proteins (GRL) in the automatic annotation procedure, they do not share the major conserved features of glutaredoxins but instead they display four conserved CxxC motives. A classification of these proteins, based on sequence similarity, gene structure and predicted cellular localization is proposed. The expression of these genes was also investigated by analyzing EST databases and Arabidopsis microarray results.

DOI: 10.1007/s11120-006-9083-7
PubMed: 16915354

Affiliations:

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Le document en format XML

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<front><div type="abstract" xml:lang="en">The annotation of the recently released Populus trichocarpa genome, has allowed us to characterize extensively the multigenic families of the redoxin proteins. Proteins with two cysteines separated by two amino acids (CxxC motif) are often involved in redox reactions by promoting the formation, reduction or isomerization of disulfide bonds or by binding prosthetic groups or metals. We report here the presence of a new protein family in higher plants, constituted of 19 members in Populus trichocarpa, 15 in Arabidopsis thaliana and 17 in Oryza sativa. These proteins are almost specific to higher plants, with only two homologous genes found in mammals and arthropoda but none in other kingdoms. While these proteins were predicted as glutaredoxin-like proteins (GRL) in the automatic annotation procedure, they do not share the major conserved features of glutaredoxins but instead they display four conserved CxxC motives. A classification of these proteins, based on sequence similarity, gene structure and predicted cellular localization is proposed. The expression of these genes was also investigated by analyzing EST databases and Arabidopsis microarray results.</div>
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Identification of a new family of plant proteins loosely related to glutaredoxins with four CxxC motives.

Identification of a new family of plant proteins loosely related to glutaredoxins with four CxxC motives.

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