Reference - Detail
| RRC ID | 15324 |
|---|---|
| Author | Uhrig RG, Moorhead GB. |
| Title | Two ancient bacterial-like PPP family phosphatases from Arabidopsis are highly conserved plant proteins that possess unique properties. |
| Journal | Plant Physiol |
| Abstract |
Protein phosphorylation, catalyzed by the opposing actions of protein kinases and phosphatases, is a cornerstone of cellular signaling and regulation. Since their discovery, protein phosphatases have emerged as highly regulated enzymes with specificity that rivals their counteracting kinase partners. However, despite years of focused characterization in mammalian and yeast systems, many protein phosphatases in plants remain poorly or incompletely characterized. Here, we describe a bioinformatic, biochemical, and cellular examination of an ancient, Bacterial-like subclass of the phosphoprotein phosphatase (PPP) family designated the Shewanella-like protein phosphatases (SLP phosphatases). The SLP phosphatase subcluster is highly conserved in all plants, mosses, and green algae, with members also found in select fungi, protists, and bacteria. As in other plant species, the nucleus-encoded Arabidopsis (Arabidopsis thaliana) SLP phosphatases (AtSLP1 and AtSLP2) lack genetic redundancy and phylogenetically cluster into two distinct groups that maintain different subcellular localizations, with SLP1 being chloroplastic and SLP2 being cytosolic. Using heterologously expressed and purified protein, the enzymatic properties of both AtSLP1 and AtSLP2 were examined, revealing unique metal cation preferences in addition to a complete insensitivity to the classic serine/threonine PPP protein phosphatase inhibitors okadaic acid and microcystin. The unique properties and high conservation of the plant SLP phosphatases, coupled to their exclusion from animals, red algae, cyanobacteria, archaea, and most bacteria, render understanding the function(s) of this new subclass of PPP family protein phosphatases of particular interest. |
| Volume | 157(4) |
| Pages | 1778-92 |
| Published | 2011-12-1 |
| DOI | 10.1104/pp.111.182493 |
| PII | pp.111.182493 |
| PMID | 21976480 |
| PMC | PMC3327225 |
| MeSH | Amino Acid Sequence Arabidopsis / enzymology* Arabidopsis / metabolism Arabidopsis Proteins / genetics Arabidopsis Proteins / isolation & purification Arabidopsis Proteins / metabolism* Base Sequence Cloning, Molecular Computational Biology Conserved Sequence Escherichia coli / genetics Escherichia coli / metabolism Microcystins / pharmacology Molecular Sequence Data Okadaic Acid / pharmacology Phosphoprotein Phosphatases / genetics Phosphoprotein Phosphatases / isolation & purification Phosphoprotein Phosphatases / metabolism* Phosphorylation Phylogeny Plant Leaves / enzymology Plant Leaves / genetics Plant Leaves / metabolism Sequence Alignment Shewanella / genetics Vicia faba / genetics Vicia faba / metabolism |
| IF | 6.902 |
| Times Cited | 19 |
| WOS Category | PLANT SCIENCES |
| Altmetric score |
オルトメトリクス指標項目
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| The most frequently cited source | Patent(IFI CLAIMS) |
| Total number of mentions | 1 |
| Altmetric score changes over past 6months | 0.0 |
| Resource | |
| Arabidopsis / Cultured plant cells, genes | pst18755 pst15755 |