Literature DB >> 18156295

Evolutionary radiation pattern of novel protein phosphatases revealed by analysis of protein data from the completely sequenced genomes of humans, green algae, and higher plants.

David Kerk1, George Templeton, Greg B G Moorhead.   

Abstract

In addition to the major serine/threonine-specific phosphoprotein phosphatase, Mg(2+)-dependent phosphoprotein phosphatase, and protein tyrosine phosphatase families, there are novel protein phosphatases, including enzymes with aspartic acid-based catalysis and subfamilies of protein tyrosine phosphatases, whose evolutionary history and representation in plants is poorly characterized. We have searched the protein data sets encoded by the well-finished nuclear genomes of the higher plants Arabidopsis (Arabidopsis thaliana) and Oryza sativa, and the latest draft data sets from the tree Populus trichocarpa and the green algae Chlamydomonas reinhardtii and Ostreococcus tauri, for homologs to several classes of novel protein phosphatases. The Arabidopsis proteins, in combination with previously published data, provide a complete inventory of known types of protein phosphatases in this organism. Phylogenetic analysis of these proteins reveals a pattern of evolution where a diverse set of protein phosphatases was present early in the history of eukaryotes, and the division of plant and animal evolution resulted in two distinct sets of protein phosphatases. The green algae occupy an intermediate position, and show similarity to both plants and animals, depending on the protein. Of specific interest are the lack of cell division cycle (CDC) phosphatases CDC25 and CDC14, and the seeming adaptation of CDC14 as a protein interaction domain in higher plants. In addition, there is a dramatic increase in proteins containing RNA polymerase C-terminal domain phosphatase-like catalytic domains in the higher plants. Expression analysis of Arabidopsis phosphatase genes differentially amplified in plants (specifically the C-terminal domain phosphatase-like phosphatases) shows patterns of tissue-specific expression with a statistically significant number of correlated genes encoding putative signal transduction proteins.

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Year:  2007        PMID: 18156295      PMCID: PMC2245839          DOI: 10.1104/pp.107.111393

Source DB:  PubMed          Journal:  Plant Physiol        ISSN: 0032-0889            Impact factor:   8.340


  79 in total

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Authors:  J Felsenstein
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Authors:  C G Koh; S H Oon; S Brenner
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5.  The structural basis for 14-3-3:phosphopeptide binding specificity.

Authors:  M B Yaffe; K Rittinger; S Volinia; P R Caron; A Aitken; H Leffers; S J Gamblin; S J Smerdon; L C Cantley
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Review 6.  Gapped BLAST and PSI-BLAST: a new generation of protein database search programs.

Authors:  S F Altschul; T L Madden; A A Schäffer; J Zhang; Z Zhang; W Miller; D J Lipman
Journal:  Nucleic Acids Res       Date:  1997-09-01       Impact factor: 16.971

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8.  An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae.

Authors:  J Archambault; R S Chambers; M S Kobor; Y Ho; M Cartier; D Bolotin; B Andrews; C M Kane; J Greenblatt
Journal:  Proc Natl Acad Sci U S A       Date:  1997-12-23       Impact factor: 11.205

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Authors:  K L Milarski; G Zhu; C G Pearl; D J McNamara; E M Dobrusin; D MacLean; A Thieme-Sefler; Z Y Zhang; T Sawyer; S J Decker
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  67 in total

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Journal:  Plant Signal Behav       Date:  2012-10-26

6.  Interfacing protein lysine acetylation and protein phosphorylation: ancient modifications meet on ancient proteins.

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Journal:  Plant Signal Behav       Date:  2012-07-25

7.  Protein phosphatase 2B (PP2B, calcineurin) in Paramecium: partial characterization reveals that two members of the unusually large catalytic subunit family have distinct roles in calcium-dependent processes.

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8.  Functional analysis in Arabidopsis of FsPTP1, a tyrosine phosphatase from beechnuts, reveals its role as a negative regulator of ABA signaling and seed dormancy and suggests its involvement in ethylene signaling modulation.

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9.  Stable isotope metabolic labeling-based quantitative phosphoproteomic analysis of Arabidopsis mutants reveals ethylene-regulated time-dependent phosphoproteins and putative substrates of constitutive triple response 1 kinase.

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10.  Crystal structure and putative substrate identification for the Entamoeba histolytica low molecular weight tyrosine phosphatase.

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