Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow E-letters: Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when E-letters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (9)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Joly, C.
Right arrow Articles by Riou-Khamlichi, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Joly, C.
Right arrow Articles by Riou-Khamlichi, C.
Agricola
Right arrow Articles by Joly, C.
Right arrow Articles by Riou-Khamlichi, C.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Journal of Experimental Botany, Vol. 53, No. 373, pp. 1429-1436, June 2002
© 2002 Oxford University Press


Original Papers

{alpha}4-Fucosyltransferase is regulated during flower development: increases in activity are targeted to pollen maturation and pollen tube elongation

Caroline Joly, Renaud Léonard, Abderrahman Maftah and Catherine Riou-Khamlichi1

Glycobiologie et Biotechnologie EA3176, Institut des Sciences de la Vie et de la Santé, Université de Limoges, 123 avenue Albert Thomas, 87060 Limoges Cedex, France

{alpha}4-Fucosylation represents a final step of protein N- glycosylation. {alpha}4-fucosylated N-glycans are thought to be involved in cell-to-cell communication and recognition in primates and plants. Nevertheless, in the plant life cycle, the function of {alpha}4-fucosylation remains largely unknown. To gain an insight into the role of {alpha}4-fucosylation during development, the study focused on tobacco flowers. It is shown that an increase in {alpha}(1,4)fucosyltransferase (Fuc-T) activity is only observed during anther development, whereas it remains at a constant but low level (around 20 pmol Fuc h-1 mg-1 protein) in the gynoecium and perianth. At least a 4-fold higher activity is detected in mature pollen grains. These data suggest that {alpha}(1,4)Fuc-T activity is regulated during anther development. Furthermore, {alpha}(1,4)Fuc-T activity could be required during pollen tube elongation where the activity level peaks at 350 pmol h-1 mg-1 protein. Based on enzyme profile and cycloheximide effects on pollen germination and activity, it is hypothesized that the gene encoding {alpha}4-Fuc-T could be regulated late during pollen development. A potential role of {alpha}4- fucosylation during pollen tube elongation is also discussed.

Key words: Elongation, fucosylation, pollen, tobacco.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
GlycobiologyHome page
B. Ma, J. L. Simala-Grant, and D. E. Taylor
Fucosylation in prokaryotes and eukaryotes
Glycobiology, December 1, 2006; 16(12): 158R - 184R.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.