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Modifying the pollen coat protein composition in Brassica
Author(s) -
Foster Elizabeth,
Schneiderman Danielle,
Cloutier Michel,
Gleddie Stephen,
Robert Laurian S.
Publication year - 2002
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.2002.01369.x
Subject(s) - tapetum , oleosin , pollen , coat , brassicaceae , biology , botany , brassica , stamen , biochemistry , gene , paleontology , microspore
Summary The interactions between pollen and stigma are essential for plant reproduction and are made possible by compounds, such as proteins and lipids, located on their surfaces. The pollen coat is formed in part by compounds synthesized in, and released from, the tapetum, which become transferred to the pollen coat late in pollen development. In the Brassicaceae the predominant proteins of the mature pollen coat are the tapetal oleosin‐like proteins, which are highly expressed in, and ultimately transferred from, the tapetum. Here we report the modification of the protein composition of the pollen coat by the addition of an active enzyme which was synthesized in the tapetum. The marker enzyme β ‐glucuronidase (GUS) was successfully targeted to the pollen coat in transgenic Brassica carinata plants expressing GUS translationally fused to a B. napus tapetal oleosin‐like protein (BnOlnB;4). To our knowledge this is the first demonstration of the targeting of an enzyme to the pollen coat.