scholarly journals Identification and Biochemical Characterization of Protein Phosphatase 5 from the Cantharidin-Producing Blister Beetle, Epicauta chinensis

2013 ◽  
Vol 14 (12) ◽  
pp. 24501-24513 ◽  
Author(s):  
Xi'en Chen ◽  
Shumin Lü ◽  
Yalin Zhang
Keyword(s):  
Protein Phosphatase ◽  
Biochemical Characterization ◽  
Protein Phosphatase 5 ◽  
Blister Beetle

scholarly journals Biochemical characterization of recombinant subunits of type 2A protein phosphatase overexpressed in Pichia pastoris

2000 ◽  
Vol 267 (16) ◽  
pp. 5209-5216 ◽  
Author(s):  
Wojciech Swiatek ◽  
Ewa Sugajska ◽  
Leszek Lankiewicz ◽  
Brian A. Hemmings ◽  
Stanislaw Zolnierowicz
Keyword(s):  
Pichia Pastoris ◽  
Protein Phosphatase ◽  
Biochemical Characterization

scholarly journals Identification and Biochemical Characterization of a Novel Protein Phosphatase 2C-Like Ser/Thr Phosphatase in Escherichia coli

2018 ◽  
Vol 200 (18) ◽  
Author(s):  
Krithika Rajagopalan ◽  
Elizabeth Nagle ◽  
Jonathan Dworkin
Keyword(s):  
Escherichia Coli ◽  
Protein Phosphatase ◽  
Biochemical Characterization ◽  
Regulatory Protein ◽  
Negative Bacterium ◽  
Gram Negative ◽  
Content Type ◽  
E Coli ◽  
Novel Protein

Regulatory protein phosphorylation is a conserved mechanism of signaling in all biological systems. Recent phosphoproteomic analyses of phylogenetically diverse bacteria, including the model Gram-negative bacteriumEscherichia coli, demonstrate that many proteins are phosphorylated on serine or threonine residues. In contrast to phosphorylation on histidine or aspartate residues, phosphorylation of serine and threonine residues is stable and requires the action of a partner Ser/Thr phosphatase to remove the modification. Although a number of Ser/Thr kinases have been reported inE. coli, no partner Ser/Thr phosphatases have been identified. Here, we biochemically characterize a novel Ser/Thr phosphatase that acts to dephosphorylate a Ser/Thr kinase that is encoded in the same operon.

scholarly journals Biochemical characterization of recombinant yeast PPZ1, a protein phosphatase involved in salt tolerance

FEBS Letters ◽  
1995 ◽  
Vol 368 (1) ◽  
pp. 39-44 ◽  
Author(s):  
Francesc Posas ◽  
Mathieu Bollen ◽  
Willy Stalmans ◽  
Joaquín Ariño
Keyword(s):  
Salt Tolerance ◽  
Protein Phosphatase ◽  
Biochemical Characterization ◽  
Recombinant Yeast

scholarly journals Structural and Biochemical Characterization of Human PR70 in Isolation and in Complex with the Scaffolding Subunit of Protein Phosphatase 2A

PLoS ONE ◽  
2014 ◽  
Vol 9 (7) ◽  
pp. e101846 ◽  
Author(s):  
Rebecca Dovega ◽  
Susan Tsutakawa ◽  
Esben M. Quistgaard ◽  
Madhanagopal Anandapadamanaban ◽  
Christian Löw ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Biochemical Characterization ◽  
Protein Phosphatase 2A ◽  
Phosphatase 2A

scholarly journals Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase.

1993 ◽  
Vol 268 (24) ◽  
pp. 17754-17761 ◽  
Author(s):  
S. Zhuo ◽  
J.C. Clemens ◽  
D.J. Hakes ◽  
D. Barford ◽  
J.E. Dixon
Keyword(s):  
Recombinant Protein ◽  
Protein Phosphatase ◽  
Biochemical Characterization

Identification and characterization of AtI-2, an Arabidopsis homologue of an ancient protein phosphatase 1 (PP1) regulatory subunit

2011 ◽  
Vol 435 (1) ◽  
pp. 73-83 ◽  
Author(s):  
George W. Templeton ◽  
Mhairi Nimick ◽  
Nicholas Morrice ◽  
David Campbell ◽  
Marilyn Goudreault ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Biochemical Characterization ◽  
Affinity Purification ◽  
Bioinformatic Analysis ◽  
Protein Phosphatase 1 ◽  
Regulatory Subunit ◽  
Identification And Characterization ◽  
Eukaryotic Genomes

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.

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