| Title |
LeRALF, a plant peptide that regulates root growth and development, specifically binds to 25 and 120 kDa cell surface membrane proteins of Lycopersicon peruvianum
|
|---|---|
| Published in |
Planta, May 2005
|
| DOI | 10.1007/s00425-004-1442-z |
| Pubmed ID | |
| Authors |
Justin M. Scheer, Gregory Pearce, Clarence A. Ryan |
| Abstract |
A photoaffinity analog of tomato leaf RALF peptide (LeRALF), (125)I-azido-LeRALF, bound saturably to tomato suspension cultured cells in the dark in a classical receptor binding assay. Classical kinetic analyses revealed that the analog interacted with a single binding site on the surface of the cells with a KD of 0.8x10(-9) M, typical of known peptide hormone-receptor interactions in both plants and animals. The (125)I-azido-LeRALF, when exposed to UVB light in the presence of the cells, strongly labeled only two proteins of 25 kDa and 120 kDa, with the 25 kDa protein being more strongly labeled than the 120 kDa protein. The cell-surface localization of the interaction was indicated, as suramin, a known inhibitor of peptide-receptor interactions, and native LeRALF peptide competed with (125)I-azido-LeRALF labeling of both proteins. Two biologically inactive LeRALF analogs were not competitors. Incubation of (125)I-azido-LeRALF with suspension cultured cells in the dark, where it was fully active, could subsequently be totally dissociated from cells by acid washes, indicating that it was interacting at the cell surface and was not internalized. The (125)I-azido-LeRALF-labeled 25 kDa and 120 kDa proteins could not be solubilized from cell membranes by methods that release peripheral proteins, indicating that they are integral membrane components. The cumulative kinetic and biochemical evidence strongly indicates that the two proteins may be components of a LeRALF receptor complex. |
Mendeley readers
The data shown below were compiled from readership statistics for 50 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Portugal | 1 | 2% |
| Germany | 1 | 2% |
| Australia | 1 | 2% |
| Unknown | 47 | 94% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 14 | 28% |
| Researcher | 5 | 10% |
| Student > Master | 5 | 10% |
| Student > Bachelor | 4 | 8% |
| Student > Doctoral Student | 4 | 8% |
| Other | 8 | 16% |
| Unknown | 10 | 20% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 29 | 58% |
| Biochemistry, Genetics and Molecular Biology | 9 | 18% |
| Computer Science | 2 | 4% |
| Chemistry | 1 | 2% |
| Unknown | 9 | 18% |
Attention Score in Context
This research output has an Altmetric Attention Score of 3. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 11 October 2011.
All research outputs
#7,454,427
of 22,789,566 outputs
Outputs from Planta
#599
of 2,718 outputs
Outputs of similar age
#20,344
of 57,582 outputs
Outputs of similar age from Planta
#4
of 21 outputs
Altmetric has tracked 22,789,566 research outputs across all sources so far. This one is in the 44th percentile – i.e., 44% of other outputs scored the same or lower than it.
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