stil, a peculiar molecule from styles, specifically dephosphorylates the pollen receptor kinase leprk2 and stimulates pollen tube growth in vitro保修期内,从风格独特的分子,专门脱去磷酸花粉受体激酶leprk2和体外刺激花粉管生长.pdf

Wengier et al. BMC Plant Biology 2010, 10:33 /1471-2229/10/33 RESEARCH ARTICLE Open Access STIL, a peculiar molecule from styles, specifically dephosphorylates the pollen receptor kinase LePRK2 and stimulates pollen tube growth in vitro 1 1 1 3,4 1,2* Diego L Wengier , María A Mazzella , Tamara M Salem , Sheila McCormick , Jorge P Muschietti 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. Background geographical position within the female tissues and In plants, pollination and subsequent fertilization rely on modify their physiology accordingly. an extensive and complex dialog between the tissues of LePRK1 and LePRK2 are tw