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Do 14-3-3 proteins and plasma membrane H+-AtPases interact in the barley epidermis in response to the barley powdery mildew fungus?
- Source :
-
Plant molecular biology [Plant Mol Biol] 2002 May; Vol. 49 (2), pp. 137-47. - Publication Year :
- 2002
-
Abstract
- 14-3-3 proteins form a family of highly conserved proteins with central roles in many eukaryotic signalling networks. In plants, they bind to and activate the plasma membrane H+-ATPase, creating a binding site for the phytotoxin fusicoccin. Barley 14-3-3 transcripts accumulate in the epidermis upon inoculation with the powdery mildew fungus. We have isolated a cDNA encoding a plasma membrane H+-ATPase (HvHAI), which is also induced by powdery mildew attack. The C-terminal domain of this H+-ATPase interacts with 14-3-3 proteins in the yeast two-hybrid system. Inoculation with the powdery mildew fungus, or treatment with fusicoccin, results in an increase in fusicoccin binding ability of barley leaf membranes. Overlay assays show a fungus-induced increase in binding of digoxygenin-labelled 14-3-3 protein to several proteins including a 100 kDa membrane protein, probably the plasma membrane H+-ATPase. These effects are seen specifically in the inoculated epidermis and not in the whole leaf. We propose that 14-3-3 proteins are involved in an epidermis-specific response to the powdery mildew fungus, possibly via an activation of the plasma membrane H+-ATPase.
- Subjects :
- 14-3-3 Proteins
Amino Acid Sequence
Ascomycota growth & development
Binding Sites
Gene Expression Regulation, Plant
Glycosides metabolism
Hordeum genetics
Hordeum microbiology
Membrane Proteins genetics
Membrane Proteins metabolism
Molecular Sequence Data
Plant Diseases microbiology
Plant Epidermis genetics
Plant Epidermis microbiology
Plant Leaves genetics
Plant Leaves metabolism
Protein Binding
Proton-Translocating ATPases genetics
Saccharomyces cerevisiae genetics
Sequence Homology, Amino Acid
Two-Hybrid System Techniques
Tyrosine 3-Monooxygenase genetics
Hordeum metabolism
Plant Epidermis metabolism
Proton-Translocating ATPases metabolism
Tyrosine 3-Monooxygenase metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0167-4412
- Volume :
- 49
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Plant molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 11999370
- Full Text :
- https://doi.org/10.1023/a:1014938417267