期刊
JOURNAL OF EXPERIMENTAL BOTANY
卷 53, 期 374, 页码 1559-1568出版社
OXFORD UNIV PRESS
DOI: 10.1093/jxb/erf010
关键词
endosperm; immunohistochemisty; ligand; protein-protein interaction; Zea mays
Three highly homologous Esr genes are expressed specifically in the embryo surrounding legion at the micropylar end of the maize endosperm. The proteins belong to a family of small hydrophilic proteins that share a conserved motive with CIv3, the ligand of the receptor-like kinase CIv1. 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.
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