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Journal of Experimental Botany, Vol. 53, No. 374, pp. 1559-1568, July 1, 2002
© 2002 Oxford University Press

Esr proteins are secreted by the cells of the embryo surrounding region

Received 21 August 2001; Accepted 14 March 2002

Jean-François Bonello1, Sandrine Sevilla-Lecoq1, Annick Berne1, Maria-Carmen Risueño2, Christian Dumas1 and Peter M. Rogowsky3,1

1 Reproduction et Développement des Plantes, UMR 5667 INRA-CNRS-ENSL-UCBL, ENS-Lyon, 46 Allée d’Italie, F-69364 Lyon Cedex 07, France
2 Organizacion Nuclear en el Desarrollo de Plantas, Centro de Investigaciones Biológicas, CSIC, Velázquez 144, 28006, Madrid, Spain

Abbreviations: BETL, basal endosperm transfer layer; DAP, days after pollination; ESR, embryo surrounding region; IPTG, isopropyl-ß-D-1-thiogalactopyranoside; PBS, phosphate buffered saline; PMSF, phenylmethanesulphonyl fluoride; PVPP, polyvinylpolypyrrolidone.

Three highly homologous Esr genes are expressed specifically in the embryo surrounding region at the micropylar end of the maize endosperm. The proteins belong to a family of small hydrophilic proteins that share a conserved motive with Clv3, the ligand of the receptor-like kinase Clv1. In this study, co-localization of Esr proteins with their mRNAs in the embryo surrounding region was shown with polyclonal antibodies recognizing all three Esr proteins. On a subcellular level the secretion of Esr proteins and their association with the cell wall was shown independently by cell fractionation, immunohistochemistry and transient expression of Gfp fusion proteins. Furthermore, a possible interaction of Esr proteins with a 35 kDa protein present in the lower half of maize kernels was suggested by in vitro affinity chromatography. Therefore Esr proteins share two characteristics with ligands of receptor-like kinases: they are released in the extracellular space and they have the capacity to form protein–protein interactions.

Key words: Key words: Endosperm, immunohistochemisty, ligand, protein–protein interaction, Zea mays.


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