Article (Scientific journals)
FIL2, an extracellular Leucine-Rich Repeat protein, is specifically expressed in Antirrhinum flowers.
Steinmayr, M.; Motte, Patrick; Sommer, H. et al.
1994In Plant Journal, 5 (4), p. 459-67
Peer Reviewed verified by ORBi
 

Files


Full Text
j.1365-313X.1994.05040459.x.pdf
Publisher postprint (5.48 MB)
Download

All documents in ORBi are protected by a user license.

Send to



Details



Keywords :
Amino Acid Sequence; Base Sequence; DNA, Complementary; Genes, Plant; Immunohistochemistry; Leucine/analysis; Molecular Sequence Data; Plant Proteins/biosynthesis/chemistry/genetics; Plants; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Subcellular Fractions/metabolism; Transcription, Genetic
Abstract :
[en] The expression of the Antirrhinum gene FIL2 is affected in mutants of the homeotic transcription factor DEFICIENS. Northern and Western blot analyses showed that FIL2 in wild-type Antirrhinum flowers is expressed weakly in the petals and more abundantly in the reproductive organs; the gene is active in the filaments and anthers of stamens, and in the stigma and transmitting tissue of the carpels. The FIL2 protein is glycosylated with high mannose type glycan chains and is located in the middle lamella of the extracellular matrix. The amino acid sequence contains 10 tandem repeats, the composition of which is similar to the Leucine-Rich Repeat (LRR) motif found in mammals, Drosophila and yeast. The possibility that FIL2 might be a component of a cellular signalling mechanism, involving LRR-mediated protein-protein interactions is discussed.
Disciplines :
Genetics & genetic processes
Author, co-author :
Steinmayr, M.
Motte, Patrick ;  Université de Liège - ULiège > Département des sciences de la vie > Génomique fonctionnelle et imagerie moléculaire végétale
Sommer, H.
Saedler, H.
Schwarz-Sommer, Z.
Language :
English
Title :
FIL2, an extracellular Leucine-Rich Repeat protein, is specifically expressed in Antirrhinum flowers.
Publication date :
1994
Journal title :
Plant Journal
ISSN :
0960-7412
eISSN :
1365-313X
Publisher :
Blackwell, Oxford, United Kingdom
Volume :
5
Issue :
4
Pages :
459-67
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 11 September 2010

Statistics


Number of views
87 (5 by ULiège)
Number of downloads
183 (3 by ULiège)

Scopus citations®
 
28
Scopus citations®
without self-citations
26
OpenCitations
 
1

Bibliography


Similar publications



Contact ORBi