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Catalytic activity of a novel serine/threonine protein phosphatase PP5 from Leishmania major

Leishmaniasis is a vector-borne disease caused by protozoan parasites of the genus Leishmania. Our knowledge of protein phosphatases (PPs) and their implication in signaling events is very limited. Here we report the expression, characterization and mutagenesis analysis of a novel protein phosphatas...

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Autores principales: Norris-Mullins, Brianna, Vacchina, Paola, Morales, Miguel A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: EDP Sciences 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4042446/
https://www.ncbi.nlm.nih.gov/pubmed/24890370
http://dx.doi.org/10.1051/parasite/2014027
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author Norris-Mullins, Brianna
Vacchina, Paola
Morales, Miguel A.
author_facet Norris-Mullins, Brianna
Vacchina, Paola
Morales, Miguel A.
author_sort Norris-Mullins, Brianna
collection PubMed
description Leishmaniasis is a vector-borne disease caused by protozoan parasites of the genus Leishmania. Our knowledge of protein phosphatases (PPs) and their implication in signaling events is very limited. Here we report the expression, characterization and mutagenesis analysis of a novel protein phosphatase 5 (PP5) in Leishmania major. Recombinant PP5 is a bona fide phosphatase and is enzymatically active. Site-directed mutagenesis revealed auto-inhibitory roles of the N-terminal region. This is a rational first approach to understand the role of PP5 in the biology of the parasite better as well as its potential future applicability to anti-parasitic intervention.
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spelling pubmed-40424462014-06-18 Catalytic activity of a novel serine/threonine protein phosphatase PP5 from Leishmania major Norris-Mullins, Brianna Vacchina, Paola Morales, Miguel A. Parasite Research Article Leishmaniasis is a vector-borne disease caused by protozoan parasites of the genus Leishmania. Our knowledge of protein phosphatases (PPs) and their implication in signaling events is very limited. Here we report the expression, characterization and mutagenesis analysis of a novel protein phosphatase 5 (PP5) in Leishmania major. Recombinant PP5 is a bona fide phosphatase and is enzymatically active. Site-directed mutagenesis revealed auto-inhibitory roles of the N-terminal region. This is a rational first approach to understand the role of PP5 in the biology of the parasite better as well as its potential future applicability to anti-parasitic intervention. EDP Sciences 2014 2014-06-04 /pmc/articles/PMC4042446/ /pubmed/24890370 http://dx.doi.org/10.1051/parasite/2014027 Text en © B. Norris-Mullins et al., published by EDP Sciences, 2014 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Norris-Mullins, Brianna
Vacchina, Paola
Morales, Miguel A.
Catalytic activity of a novel serine/threonine protein phosphatase PP5 from Leishmania major
title Catalytic activity of a novel serine/threonine protein phosphatase PP5 from Leishmania major
title_full Catalytic activity of a novel serine/threonine protein phosphatase PP5 from Leishmania major
title_fullStr Catalytic activity of a novel serine/threonine protein phosphatase PP5 from Leishmania major
title_full_unstemmed Catalytic activity of a novel serine/threonine protein phosphatase PP5 from Leishmania major
title_short Catalytic activity of a novel serine/threonine protein phosphatase PP5 from Leishmania major
title_sort catalytic activity of a novel serine/threonine protein phosphatase pp5 from leishmania major
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4042446/
https://www.ncbi.nlm.nih.gov/pubmed/24890370
http://dx.doi.org/10.1051/parasite/2014027
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