Reversible phosphorylation of a protein from Trypanosoma equiperdum that exhibits homology with the regulatory subunits of mammalian cAMP-dependent protein kinases

Escalona, José L.; Bubis, José

doi:10.1016/j.biochi.2020.12.018

Biochimie

2021

DOI: 10.1016/j.biochi.2020.12.018

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Reversible phosphorylation of a protein from Trypanosoma equiperdum that exhibits homology with the regulatory subunits of mammalian cAMP-dependent protein kinases

José L. Escalona

José Bubis

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Cited by 2 publications

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Analysis of a Novel Peptide That Is Capable of Inhibiting the Enzymatic Activity of the Protein Kinase A Catalytic Subunit-Like Protein from Trypanosoma equiperdum

Araujo,

Bubis

2023

Protein J

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A peptide possessing the αN-helix motif of the protein kinase A (PKA) regulatory subunit-like protein from the Trypanozoom subgenera (VAP26) was shown to inhibit the enzymatic activity of the Trypanosoma equiperdumPKA catalytic subunit-like protein in a similar manner that the mammalian heat-stable soluble PKA inhibitor (PKI). However, VAP26 did not contain the PKI inhibitory sequence. Bioinformatics analyzes of the αN-helix motif from the Trypanozoon protein suggested that the sequence can form favorable peptide-protein interactions of hydrophobic nature with the PKA catalytic subunit-like protein, which could represent an alternative PKA inhibition mechanism. It was determined that the sequence of the αN-helix motif of the Trypanozoon protein is conserved but signi cantly divergent from the corresponding αN-helix motifs in the Leishmania and mammalian proteins. This sequence divergence contrasted with the secondary structure of the αN-helix motif, which appeared to be conserved in every regulatory subunit-like protein that was analyzed. In silico mutation experiments at positions I234, L238 and F244 of the αNhelix motif from the Trypanozoon protein destabilized both the speci c motif and the protein, while mutations at positions T239 and Y240, on the contrary, stabilized the motif and the protein. These results suggested that the αN-helix motif from the Trypanozoon protein probably possessed a different evolutionary path than its Leishmania and mammalian counterparts. Moreover, nding stabilizing mutations can be used for the design of novel inhibitory peptides on the basis of the αN-helix motif from the Trypanozoon PKA regulatory subunit-like protein.

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Analysis of a Novel Peptide That Is Capable of Inhibiting the Enzymatic Activity of the Protein Kinase A Catalytic Subunit-Like Protein from Trypanosoma equiperdum

Araujo,

Bubis

2023

Protein J

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Cloning, expression, solubilization, and purification of a functionally active recombinant cAMP-dependent protein kinase catalytic subunit-like protein PKAC1 from Trypanosoma equiperdum

Guevara

Lugo

Montilla

et al. 2022

Protein Expression and Purification

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Reversible phosphorylation of a protein from Trypanosoma equiperdum that exhibits homology with the regulatory subunits of mammalian cAMP-dependent protein kinases

Cited by 2 publications

References 39 publications

Analysis of a Novel Peptide That Is Capable of Inhibiting the Enzymatic Activity of the Protein Kinase A Catalytic Subunit-Like Protein from Trypanosoma equiperdum

Analysis of a Novel Peptide That Is Capable of Inhibiting the Enzymatic Activity of the Protein Kinase A Catalytic Subunit-Like Protein from Trypanosoma equiperdum

Cloning, expression, solubilization, and purification of a functionally active recombinant cAMP-dependent protein kinase catalytic subunit-like protein PKAC1 from Trypanosoma equiperdum

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