A novel phloem-specific gene is expressed preferentially in aerial portions of Vicia faba

We have isolated a gene from bean (Vicia faba L.), called Vein1, that encodes a novel protein. The Vein1 cDNA was isolated as a result of a differential screen for genes that are expressed in leaves but not in the most common cell type, the mesophyll cell. Northern blot analysis revealed that Vein 1...

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Bibliographic Details
Published in:Plant molecular biology 1996-02, Vol.30 (4), p.687-695
Main Authors: Foley, R C, Liang, Z M, Singh, K B
Format: Article
Language:English
Subjects:
adn
Amino Acid Sequence
Base Sequence
calice
caliz
calyx
corola
corolla
corolle
dna
DNA, Complementary - genetics
expresion genica
expression des genes
Fabaceae - anatomy & histology
Fabaceae - chemistry
Fabaceae - genetics
feuille
floema
Gene Expression
Genes, Plant
histidina
histidine
hojas
In Situ Hybridization
leaves
mesofilo
mesophyll
mesophylle
Molecular Probe Techniques
Molecular Sequence Data
phloem
phloeme
Plant Proteins - biosynthesis
Plant Proteins - genetics
Plant Shoots - anatomy & histology
Plant Shoots - chemistry
Plant Stems - chemistry
Plants, Medicinal
Protein Conformation
racine
raices
roots
Sequence Analysis, DNA
stems
tallo
tige
Tissue Distribution
Vicia faba
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Description
Summary:We have isolated a gene from bean (Vicia faba L.), called Vein1, that encodes a novel protein. The Vein1 cDNA was isolated as a result of a differential screen for genes that are expressed in leaves but not in the most common cell type, the mesophyll cell. Northern blot analysis revealed that Vein 1 transcripts are differentially expressed in the plant with expression in leaves, stems and sepals but not in petals, mesophyll cells or roots. In situ hybridization studies of stem and leaf sections indicate that the expression of Vein1 is localized to the phloem tissue. Interestingly, Vein1 was differentially expressed in stem tissue with the highest expression in the oldest internodes. The deduced Vein1 protein sequence does not share homology with any known protein sequences. The 17 kDa Vein1 protein is highly hydrophilic and contains a histidine-rich motif, where six out of seven amino acids are histidines. The function of Vein1 is unknown, although the expression patterns suggests that it may play a role in mature phloem tissue in the aerial parts of the plant.
ISSN:0167-4412
1573-5028
DOI:10.1007/BF00019004