Modifying the pollen coat protein composition in Brassica.
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 beta-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.
Foster
Elizabeth
E
Eastern Cereal and Oilseed Research Centre, Agriculture and Agri-Food Canada, 2091 K.W. Neatby Bldg., 960 Carling Ave., Ottawa, ON K1A 0C6, Canada.
Schneiderman
Danielle
D
Cloutier
Michel
M
Gleddie
Stephen
S
Robert
Laurian S
LS
D001937:Brassica / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D018507:Gene Expression Regulation, Developmental; D018506:Gene Expression Regulation, Plant; D005966:Glucuronidase / Q000235:genetics / Q000378:metabolism; D016253:Microscopy, Immunoelectron; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D030821:Plants, Genetically Modified; D011058:Pollen / Q000254:growth & development / Q000378:metabolism* / Q000648:ultrastructure; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D012098:Reproduction / Q000502:physiology
D010940:Plant Proteins; D011993:Recombinant Fusion Proteins; C079356:oleosin protein, Brassica napus; D005966:Glucuronidase