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Abstract:

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.

Registro:

Documento: Artículo
Título:STIL, a peculiar molecule from styles, specifically dephosphorylates the pollen receptor kinase LePRK2 and stimulates pollen tube growth in vitro
Autor:Wengier, D.L.; Mazzella, M.A.; Salem, T.M.; McCormick, S.; Muschietti, J.P.
Filiación:Instituto de Ingeniería Genética y Biología Molecular (INGEBI), CONICET, Vuelta de Obligado 2490, 1428 Buenos Aires, Argentina
Departamento de Fisiología y Biología Molecular y Celular, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina
Plant Gene Expression Center, United States Department of Agriculture/Agricultural Research Service, 800 Buchanan Street, Albany, CA 94710, United States
Department of Plant and Microbial Biology, University of California at Berkeley, Berkeley, CA 94720, United States
Palabras clave: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
Año:2010
Volumen:10
DOI: http://dx.doi.org/10.1186/1471-2229-10-33
Título revista:BMC Plant Biology
Título revista abreviado:BMC Plant Biol.
ISSN:14712229
CAS:protein kinase C, 141436-78-4; Plant Proteins; Protein Kinase C, 2.7.11.13; protein kinase N, 2.7.1.-
PDF:https://bibliotecadigital.exactas.uba.ar/download/paper/paper_14712229_v10_n_p_Wengier.pdf
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14712229_v10_n_p_Wengier

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Citas:

---------- APA ----------
Wengier, D.L., Mazzella, M.A., Salem, T.M., McCormick, S. & Muschietti, J.P. (2010) . STIL, a peculiar molecule from styles, specifically dephosphorylates the pollen receptor kinase LePRK2 and stimulates pollen tube growth in vitro. BMC Plant Biology, 10.
http://dx.doi.org/10.1186/1471-2229-10-33
---------- CHICAGO ----------
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" . BMC Plant Biology 10 (2010).
http://dx.doi.org/10.1186/1471-2229-10-33
---------- MLA ----------
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" . BMC Plant Biology, vol. 10, 2010.
http://dx.doi.org/10.1186/1471-2229-10-33
---------- VANCOUVER ----------
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. BMC Plant Biol. 2010;10.
http://dx.doi.org/10.1186/1471-2229-10-33