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Identification and characterization of AtI-2, an Arabidopsis homologue of an ancient protein phosphatase 1 (PP1) regulatory subunit
- Source :
- Biochemical Journal. 435:73-83
- Publication Year :
- 2011
- Publisher :
- Portland Press Ltd., 2011.
-
Abstract
- PP1 (protein phosphatase 1) is among the most conserved enzymes known, with one or more isoforms present in all sequenced eukaryotic genomes. PP1 dephosphorylates specific serine/threonine phosphoproteins as defined by associated regulatory or targeting subunits. In the present study we performed a PP1-binding screen to find putative PP1 interactors in Arabidopsis thaliana and uncovered a homologue of the ancient PP1 interactor, I-2 (inhibitor-2). Bioinformatic analysis revealed remarkable conservation of three regions of plant I-2 that play key roles in binding to PP1 and regulating its function. The sequence-related properties of plant I-2 were compared across eukaryotes, indicating a lack of I-2 in some species and the emergence points from key motifs during the evolution of this ancient regulator. Biochemical characterization of AtI-2 (Arabidopsis I-2) revealed its ability to inhibit all plant PP1 isoforms and inhibitory dependence requiring the primary interaction motif known as RVXF. Arabidopsis I-2 was shown to be a phosphoprotein in vivo that was enriched in the nucleus. TAP (tandem affinity purification)-tag experiments with plant I-2 showed in vivo association with several Arabidopsis PP1 isoforms and identified other potential I-2 binding proteins.
- Subjects :
- Gene isoform
Recombinant Fusion Proteins
Protein subunit
Molecular Sequence Data
Arabidopsis
macromolecular substances
Biochemistry
DNA-binding protein
Cell Line
Plant Epidermis
Serine
Protein Phosphatase 1
Protein Isoforms
Amino Acid Sequence
Databases, Protein
Molecular Biology
Phylogeny
Cell Nucleus
Genetics
Tandem affinity purification
Sequence Homology, Amino Acid
biology
Arabidopsis Proteins
fungi
Computational Biology
food and beverages
Protein phosphatase 1
Cell Biology
Phosphoproteins
biology.organism_classification
Cell biology
Plant Leaves
Protein Subunits
Protein Transport
Phosphoprotein
Plant Structures
Sequence Alignment
Subjects
Details
- ISSN :
- 14708728 and 02646021
- Volume :
- 435
- Database :
- OpenAIRE
- Journal :
- Biochemical Journal
- Accession number :
- edsair.doi.dedup.....4d272687140e269f5596f43eaa281a39