STIL, a peculiar molecule from styles, specifically dephosphorylates the pollen receptor kinase LePRK2 and stimulates pollen tube growth in vitro
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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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14712229_v10_n_p_Wengier http://hdl.handle.net/20.500.12110/paper_14712229_v10_n_p_Wengier |
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paper:paper_14712229_v10_n_p_Wengier2023-06-08T16:17:16Z STIL, a peculiar molecule from styles, specifically dephosphorylates the pollen receptor kinase LePRK2 and stimulates pollen tube growth in vitro Wengier, Diego Leonardo Mazzella, María Agustina Salem, Tamara Marcela Muschietti, Jorge 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 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14712229_v10_n_p_Wengier 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, Diego Leonardo Mazzella, María Agustina Salem, Tamara Marcela Muschietti, Jorge 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. |
| author |
Wengier, Diego Leonardo Mazzella, María Agustina Salem, Tamara Marcela Muschietti, Jorge P. |
| author_facet |
Wengier, Diego Leonardo Mazzella, María Agustina Salem, Tamara Marcela Muschietti, Jorge P. |
| author_sort |
Wengier, Diego Leonardo |
| 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 |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14712229_v10_n_p_Wengier http://hdl.handle.net/20.500.12110/paper_14712229_v10_n_p_Wengier |
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