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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
EDP Sciences
2014
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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. |
format | Online Article Text |
id | pubmed-4042446 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | EDP Sciences |
record_format | MEDLINE/PubMed |
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
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title_full | Catalytic activity of a novel serine/threonine protein phosphatase PP5 from Leishmania major
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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
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title_short | Catalytic activity of a novel serine/threonine protein phosphatase PP5 from Leishmania major
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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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