STIL, a peculiar molecule from styles, specifically dephosphorylates the pollen receptor kinase LePRK2 and stimulates pollen tube growth in vitro

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Background: LePRK1 and LePRK2 are two pollen receptor kinases localized to the plasma membrane, where they are present in a high molecular weight complex (LePRK complex). LePRK2 is phosphorylated in mature and germinated pollen, but is dephosphorylated when pollen membranes are incubated with tomato...

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Autores principales: Wengier, D.L., Mazzella, M.A., Salem, T.M., McCormick, S., Muschietti, J.P.
Formato: Artículo publishedVersion
Lenguaje:Inglés
Publicado: 2010
Materias:
Lycopersicon esculentum
Nicotiana tabacum
protein kinase C
protein kinase N
vegetable protein
article
genetics
growth, development and aging
isolation and purification
metabolism
phosphorylation
pollen tube
tomato
Phosphorylation
Plant Proteins
Pollen Tube
Protein Kinase C
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_14712229_v10_n_p_Wengier
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paperaa:paper_14712229_v10_n_p_Wengier
record_format dspace
spelling paperaa:paper_14712229_v10_n_p_Wengier2023-06-12T16:50:26Z STIL, a peculiar molecule from styles, specifically dephosphorylates the pollen receptor kinase LePRK2 and stimulates pollen tube growth in vitro BMC Plant Biol. 2010;10 Wengier, D.L. Mazzella, M.A. Salem, T.M. McCormick, S. Muschietti, J.P. Lycopersicon esculentum Nicotiana tabacum protein kinase C protein kinase N vegetable protein article genetics growth, development and aging isolation and purification metabolism phosphorylation pollen tube tomato Lycopersicon esculentum Phosphorylation Plant Proteins Pollen Tube Protein Kinase C Background: LePRK1 and LePRK2 are two pollen receptor kinases localized to the plasma membrane, where they are present in a high molecular weight complex (LePRK complex). LePRK2 is phosphorylated in mature and germinated pollen, but is dephosphorylated when pollen membranes are incubated with tomato or tobacco style extracts.Results: Here we show that LePRK2 dephosphorylation is mediated by a heat-, acid-, base-, DTT- and protease-resistant component from tobacco styles. Using LePRK2 phosphorylation as a tracking assay for purification, style exudates were subjected to chloroform extraction, anionic exchange, and C18 reverse-phase chromatography columns. We finally obtained a single ~3,550 Da compound (as determined by UV-MALDI-TOF MS) that we named STIL (for Style Interactor for LePRKs). STIL increased pollen tube lengths of in vitro germinated pollen in a dose-dependent manner.Conclusion: We propose that the LePRK complex perceives STIL, resulting in LePRK2 dephosphorylation and an increase in pollen tube growth. © 2010 Wengier et al; licensee BioMed Central Ltd. Fil:Wengier, D.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Mazzella, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Salem, T.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Muschietti, J.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2010 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion application/pdf eng info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_14712229_v10_n_p_Wengier
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
language Inglés
orig_language_str_mv eng
topic Lycopersicon esculentum
Nicotiana tabacum
protein kinase C
protein kinase N
vegetable protein
article
genetics
growth, development and aging
isolation and purification
metabolism
phosphorylation
pollen tube
tomato
Lycopersicon esculentum
Phosphorylation
Plant Proteins
Pollen Tube
Protein Kinase C
spellingShingle Lycopersicon esculentum
Nicotiana tabacum
protein kinase C
protein kinase N
vegetable protein
article
genetics
growth, development and aging
isolation and purification
metabolism
phosphorylation
pollen tube
tomato
Lycopersicon esculentum
Phosphorylation
Plant Proteins
Pollen Tube
Protein Kinase C
Wengier, D.L.
Mazzella, M.A.
Salem, T.M.
McCormick, S.
Muschietti, J.P.
STIL, a peculiar molecule from styles, specifically dephosphorylates the pollen receptor kinase LePRK2 and stimulates pollen tube growth in vitro
topic_facet Lycopersicon esculentum
Nicotiana tabacum
protein kinase C
protein kinase N
vegetable protein
article
genetics
growth, development and aging
isolation and purification
metabolism
phosphorylation
pollen tube
tomato
Lycopersicon esculentum
Phosphorylation
Plant Proteins
Pollen Tube
Protein Kinase C
description Background: LePRK1 and LePRK2 are two pollen receptor kinases localized to the plasma membrane, where they are present in a high molecular weight complex (LePRK complex). LePRK2 is phosphorylated in mature and germinated pollen, but is dephosphorylated when pollen membranes are incubated with tomato or tobacco style extracts.Results: Here we show that LePRK2 dephosphorylation is mediated by a heat-, acid-, base-, DTT- and protease-resistant component from tobacco styles. Using LePRK2 phosphorylation as a tracking assay for purification, style exudates were subjected to chloroform extraction, anionic exchange, and C18 reverse-phase chromatography columns. We finally obtained a single ~3,550 Da compound (as determined by UV-MALDI-TOF MS) that we named STIL (for Style Interactor for LePRKs). STIL increased pollen tube lengths of in vitro germinated pollen in a dose-dependent manner.Conclusion: We propose that the LePRK complex perceives STIL, resulting in LePRK2 dephosphorylation and an increase in pollen tube growth. © 2010 Wengier et al; licensee BioMed Central Ltd.
format Artículo
Artículo
publishedVersion
author Wengier, D.L.
Mazzella, M.A.
Salem, T.M.
McCormick, S.
Muschietti, J.P.
author_facet Wengier, D.L.
Mazzella, M.A.
Salem, T.M.
McCormick, S.
Muschietti, J.P.
author_sort Wengier, D.L.
title STIL, a peculiar molecule from styles, specifically dephosphorylates the pollen receptor kinase LePRK2 and stimulates pollen tube growth in vitro
title_short STIL, a peculiar molecule from styles, specifically dephosphorylates the pollen receptor kinase LePRK2 and stimulates pollen tube growth in vitro
title_full STIL, a peculiar molecule from styles, specifically dephosphorylates the pollen receptor kinase LePRK2 and stimulates pollen tube growth in vitro
title_fullStr STIL, a peculiar molecule from styles, specifically dephosphorylates the pollen receptor kinase LePRK2 and stimulates pollen tube growth in vitro
title_full_unstemmed STIL, a peculiar molecule from styles, specifically dephosphorylates the pollen receptor kinase LePRK2 and stimulates pollen tube growth in vitro
title_sort stil, a peculiar molecule from styles, specifically dephosphorylates the pollen receptor kinase leprk2 and stimulates pollen tube growth in vitro
publishDate 2010
url http://hdl.handle.net/20.500.12110/paper_14712229_v10_n_p_Wengier
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