Characterization of Protein Phosphatase 5 from Three Lepidopteran Insects: Helicoverpa armigera, Mythimna separata and Plutella xylostella

Characterization of Protein Phosphatase 5 from Three Lepidopteran Insects: Helicoverpa armigera, Mythimna separata and Plutella xylostella

Protein phosphatase 5 (PP5), a unique member of serine/threonine phosphatases, regulates a variety of biological processes. We obtained full-length PP5 cDNAs from three lepidopteran insects, Helicoverpa armigera, Mythimna separata and Plutella xylostella, encoding predicted proteins of 490 (55.98 kD...

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Main Authors: Chen, Xi’en, Lü, Shumin, Zhang, Yalin
Format: Online
Language:English
Published: Public Library of Science 2014
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4019573/
id pubmed-4019573
recordtype oai_dc
spelling pubmed-40195732014-05-16 Characterization of Protein Phosphatase 5 from Three Lepidopteran Insects: Helicoverpa armigera, Mythimna separata and Plutella xylostella Chen, Xi’en Lü, Shumin Zhang, Yalin Research Article Protein phosphatase 5 (PP5), a unique member of serine/threonine phosphatases, regulates a variety of biological processes. We obtained full-length PP5 cDNAs from three lepidopteran insects, Helicoverpa armigera, Mythimna separata and Plutella xylostella, encoding predicted proteins of 490 (55.98 kDa), 490 (55.82 kDa) and 491 (56.07 kDa) amino acids, respectively. These sequences shared a high identity with other insect PP5s and contained the TPR (tetratricopeptide repeat) domains at N-terminal regions and highly conserved C-terminal catalytic domains. Tissue- and stage-specific expression pattern analyses revealed these three PP5 genes were constitutively expressed in all stages and in tested tissues with predominant transcription occurring at the egg and adult stages. Activities of Escherichia coli-produced recombinant PP5 proteins could be enhanced by almost 2-fold by a known PP5 activator: arachidonic acid. Kinetic parameters of three recombinant proteins against substrate pNPP were similar both in the absence or presence of arachidonic acid. Protein phosphatases inhibitors, okadaic acid, cantharidin, and endothall strongly impeded the activities of the three recombinant PP5 proteins, as well as exerted an inhibitory effect on crude protein phosphatases extractions from these three insects. In summary, lepidopteran PP5s share similar characteristics and are all sensitive to the protein phosphatases inhibitors. Our results also imply protein phosphatase inhibitors might be used in the management of lepidopteran pests. Public Library of Science 2014-05-13 /pmc/articles/PMC4019573/ /pubmed/24823652 http://dx.doi.org/10.1371/journal.pone.0097437 Text en © 2014 Chen et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Chen, Xi’en
Lü, Shumin
Zhang, Yalin
spellingShingle Chen, Xi’en
Lü, Shumin
Zhang, Yalin
Characterization of Protein Phosphatase 5 from Three Lepidopteran Insects: Helicoverpa armigera, Mythimna separata and Plutella xylostella
author_facet Chen, Xi’en
Lü, Shumin
Zhang, Yalin
author_sort Chen, Xi’en
title Characterization of Protein Phosphatase 5 from Three Lepidopteran Insects: Helicoverpa armigera, Mythimna separata and Plutella xylostella
title_short Characterization of Protein Phosphatase 5 from Three Lepidopteran Insects: Helicoverpa armigera, Mythimna separata and Plutella xylostella
title_full Characterization of Protein Phosphatase 5 from Three Lepidopteran Insects: Helicoverpa armigera, Mythimna separata and Plutella xylostella
title_fullStr Characterization of Protein Phosphatase 5 from Three Lepidopteran Insects: Helicoverpa armigera, Mythimna separata and Plutella xylostella
title_full_unstemmed Characterization of Protein Phosphatase 5 from Three Lepidopteran Insects: Helicoverpa armigera, Mythimna separata and Plutella xylostella
title_sort characterization of protein phosphatase 5 from three lepidopteran insects: helicoverpa armigera, mythimna separata and plutella xylostella
description Protein phosphatase 5 (PP5), a unique member of serine/threonine phosphatases, regulates a variety of biological processes. We obtained full-length PP5 cDNAs from three lepidopteran insects, Helicoverpa armigera, Mythimna separata and Plutella xylostella, encoding predicted proteins of 490 (55.98 kDa), 490 (55.82 kDa) and 491 (56.07 kDa) amino acids, respectively. These sequences shared a high identity with other insect PP5s and contained the TPR (tetratricopeptide repeat) domains at N-terminal regions and highly conserved C-terminal catalytic domains. Tissue- and stage-specific expression pattern analyses revealed these three PP5 genes were constitutively expressed in all stages and in tested tissues with predominant transcription occurring at the egg and adult stages. Activities of Escherichia coli-produced recombinant PP5 proteins could be enhanced by almost 2-fold by a known PP5 activator: arachidonic acid. Kinetic parameters of three recombinant proteins against substrate pNPP were similar both in the absence or presence of arachidonic acid. Protein phosphatases inhibitors, okadaic acid, cantharidin, and endothall strongly impeded the activities of the three recombinant PP5 proteins, as well as exerted an inhibitory effect on crude protein phosphatases extractions from these three insects. In summary, lepidopteran PP5s share similar characteristics and are all sensitive to the protein phosphatases inhibitors. Our results also imply protein phosphatase inhibitors might be used in the management of lepidopteran pests.
publisher Public Library of Science
publishDate 2014
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4019573/
_version_ 1612088477116006400

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