Evaluation and classification of RING-finger domains encoded by the Arabidopsis genome.
Détails
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Accès restreint UNIL
Etat: Public
Version: Final published version
Licence: Non spécifiée
Accès restreint UNIL
Etat: Public
Version: Final published version
Licence: Non spécifiée
ID Serval
serval:BIB_E620AD512BEB
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Evaluation and classification of RING-finger domains encoded by the Arabidopsis genome.
Périodique
Genome biology
ISSN
1474-760X (Electronic)
ISSN-L
1474-7596
Statut éditorial
Publié
Date de publication
2002
Peer-reviewed
Oui
Volume
3
Numéro
4
Pages
RESEARCH0016
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Publication Status: ppublish
Résumé
In computational analysis, the RING-finger domain is one of the most frequently detected domains in the Arabidopsis proteome. In fact, it is more abundant in Arabidopsis than in other eukaryotic genomes. However, computational analysis might classify ambiguous domains of the closely related PHD and LIM motifs as RING domains by mistake. Thus, we set out to define an ordered set of Arabidopsis RING domains by evaluating predicted domains on the basis of recent structural data.
Inspection of the proteome with a current InterPro release predicts 446 RING domains. We evaluated each detected domain and as a result eliminated 59 false positives. The remaining 387 domains were grouped by cluster analysis and according to their metal-ligand arrangement. We further defined novel patterns for additional computational analyses of the proteome. They were based on recent structural data that enable discrimination between the related RING, PHD and LIM domains. These patterns allow us to predict with different degrees of certainty whether a particular domain is indeed likely to form a RING finger.
In summary, 387 domains have a significant potential to form a RING-type cross-brace structure. Many of these RING domains overlap with predicted PHD domains; however, the RING domain signature mostly prevails. Thus, the abundance of PHD domains in Arabidopsis has been significantly overestimated. Cluster analysis of the RING domains defines groups of proteins, which frequently show significant similarity outside the RING domain. These groups document a common evolutionary origin of their members and potentially represent genes of overlapping functionality.
Inspection of the proteome with a current InterPro release predicts 446 RING domains. We evaluated each detected domain and as a result eliminated 59 false positives. The remaining 387 domains were grouped by cluster analysis and according to their metal-ligand arrangement. We further defined novel patterns for additional computational analyses of the proteome. They were based on recent structural data that enable discrimination between the related RING, PHD and LIM domains. These patterns allow us to predict with different degrees of certainty whether a particular domain is indeed likely to form a RING finger.
In summary, 387 domains have a significant potential to form a RING-type cross-brace structure. Many of these RING domains overlap with predicted PHD domains; however, the RING domain signature mostly prevails. Thus, the abundance of PHD domains in Arabidopsis has been significantly overestimated. Cluster analysis of the RING domains defines groups of proteins, which frequently show significant similarity outside the RING domain. These groups document a common evolutionary origin of their members and potentially represent genes of overlapping functionality.
Mots-clé
Amino Acid Motifs, Arabidopsis/genetics, Arabidopsis Proteins/chemistry, Arabidopsis Proteins/classification, Computational Biology, Genome, Plant, Molecular Sequence Data, Protein Structure, Tertiary, Proteome/analysis, Sequence Analysis, Protein
Pubmed
Open Access
Oui
Création de la notice
24/01/2008 19:51
Dernière modification de la notice
09/08/2024 13:10