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: JOUR
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 todo:paper_14712229_v10_n_p_Wengier
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spelling todo:paper_14712229_v10_n_p_Wengier2023-10-03T16:17:48Z STIL, a peculiar molecule from styles, specifically dephosphorylates the pollen receptor kinase LePRK2 and stimulates pollen tube growth in vitro 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. JOUR 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)
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 JOUR
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
url http://hdl.handle.net/20.500.12110/paper_14712229_v10_n_p_Wengier
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