The unique serine/threonine phosphatase from the minimal bacterium Mycoplasma synoviae
biochemical characterization and metal dependence
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| 008 | 210128e20150101xx s 000 0 eng | ||
| 024 | 7 | 0 | |a 10.1007/s00775-014-1209-3 |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00775-014-1209-3 | ||
| 245 | 0 | 4 | |a The unique serine/threonine phosphatase from the minimal bacterium Mycoplasma synoviae |h [Elektronische Daten] |b biochemical characterization and metal dependence |c [Angela Menegatti, Javier Vernal, Hernán Terenzi] |
| 520 | 3 | |a Serine/threonine protein phosphatases have been described in many pathogenic bacteria as essential enzymes involved in phosphorylation-dependent signal transduction pathways and frequently associated with the virulence of these organisms. An inspection of Mycoplasma synoviae genome revealed the presence of a gene (prpC) encoding a putative protein phosphatase of the protein phosphatase 2C (PP2C) subfamily. Here, we report a complete biochemical characterization of M. synoviae phosphatase (PrpC) and the particular role of metal ions in the structure-function relationship of this enzyme. PrpC amino acid sequence analysis revealed that all the residues involved in the dinuclear metal center and the putative third metal ion-coordinating residues, conserved in PP2C phosphatases, are present in PrpC. PrpC is a monomeric protein able to dephosphorylate phospho-substrates with Mn2+ ions' dependence. Thermal stability analysis demonstrated the enzyme stability at mild temperatures and the influence of Mn2+ ions in this property. Mass spectrometry analysis suggested that three metal ions bind to PrpC, two of which with an apparent high-affinity constant. Mutational analysis of the putative third metal-coordinating residues, Asp122 and Arg164, revealed that these variants exhibited a weaker binding of manganese ions, and that both mutations affected PrpC phosphatase activity. According to these results, PrpC is a metal-dependent protein phosphatase member with an improved stability in the holo form and with Asp122, possibly implicated in the third metal-binding site, essential to catalytic activity. | |
| 540 | |a SBIC, 2014 | ||
| 690 | 7 | |a PP2C-like phosphatase |2 nationallicence | |
| 690 | 7 | |a Metal binding |2 nationallicence | |
| 690 | 7 | |a Mn2+ ion |2 nationallicence | |
| 690 | 7 | |a Mycoplasma synoviae |2 nationallicence | |
| 690 | 7 | |a PrpC |2 nationallicence | |
| 690 | 7 | |a ESI-MS : Electrospray ionization-mass spectrometry |2 nationallicence | |
| 690 | 7 | |a HAD : Haloacid dehalogenase |2 nationallicence | |
| 690 | 7 | |a MALDI-TOF/TOF : Matrix-assisted laser desorption/ionization-time-of-flight |2 nationallicence | |
| 690 | 7 | |a Mw : Molecular weight |2 nationallicence | |
| 690 | 7 | |a FCP/SCP : [TFIIF(transcription initiation factor IIF)-associating component of CTD (C-terminal domain) phosphatase/small CTD phosphatase] |2 nationallicence | |
| 690 | 7 | |a WT : Wild type |2 nationallicence | |
| 700 | 1 | |a Menegatti |D Angela |u Departamento de Bioquímica-CCB, Centro de Biologia Molecular Estrutural, Universidade Federal de Santa Catarina, 88040-900, Florianópolis, SC, Brazil |4 aut | |
| 700 | 1 | |a Vernal |D Javier |u Departamento de Bioquímica-CCB, Centro de Biologia Molecular Estrutural, Universidade Federal de Santa Catarina, 88040-900, Florianópolis, SC, Brazil |4 aut | |
| 700 | 1 | |a Terenzi |D Hernán |u Departamento de Bioquímica-CCB, Centro de Biologia Molecular Estrutural, Universidade Federal de Santa Catarina, 88040-900, Florianópolis, SC, Brazil |4 aut | |
| 773 | 0 | |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/1(2015-01-01), 61-75 |x 0949-8257 |q 20:1<61 |1 2015 |2 20 |o 775 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00775-014-1209-3 |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a research-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00775-014-1209-3 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Menegatti |D Angela |u Departamento de Bioquímica-CCB, Centro de Biologia Molecular Estrutural, Universidade Federal de Santa Catarina, 88040-900, Florianópolis, SC, Brazil |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Vernal |D Javier |u Departamento de Bioquímica-CCB, Centro de Biologia Molecular Estrutural, Universidade Federal de Santa Catarina, 88040-900, Florianópolis, SC, Brazil |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Terenzi |D Hernán |u Departamento de Bioquímica-CCB, Centro de Biologia Molecular Estrutural, Universidade Federal de Santa Catarina, 88040-900, Florianópolis, SC, Brazil |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/1(2015-01-01), 61-75 |x 0949-8257 |q 20:1<61 |1 2015 |2 20 |o 775 | ||