Proteomic Comparison of Needles from Blister Rust-Resistant and Susceptible Pinus strobus Seedlings Reveals UpRegulation of Putative Disease Resistance Proteins
| Autor: | Jason A. Smith, Robert A. Blanchette, Todd A. Burnes, James J. Jacobs, LeeAnn Higgins, Bruce A. Witthuhn, Andrew J. David, Jeffrey H. Gillman |
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| Jazyk: | angličtina |
| Rok vydání: | 2006 |
| Předmět: | |
| Zdroj: | Molecular Plant-Microbe Interactions, Vol 19, Iss 2, Pp 150-160 (2006) |
| Druh dokumentu: | article |
| ISSN: | 1943-7706 0894-0282 |
| DOI: | 10.1094/MPMI-19-0150 |
| Popis: | In order to characterize a hypersensitive-like reaction in selected Pinus strobus seedlings to Cronartium ribicola, a proteomic comparison of needles from resistant and susceptible seedlings was undertaken using two-dimensional gel electrophoresis (2-DE). The results revealed 19 polypeptides specific to resistant seedlings and seven of these specific to infected resistant seedlings. There were 13 polypeptides up-regulated (≥3-fold increase) in resistant family P327 in comparison to needle tissue from susceptible and mock-inoculated seedlings. Electrospray ionization liquid chromatography and tandem mass spectrometry was used to sequence 11 proteins from the 2-DE gels. Sequences obtained from electrospray ionization liquid chromatography and tandem mass spectrometry were used for MS-BLAST and Pro-ID database searches allowing identification with a 95 to 99% confidence level. Six proteins were determined to be homologs of proteins with known roles in disease resistance, five were determined to be homologs of members of the leucine-rich repeat (LRR) superfamily, and one was a homolog of heat shock protein 90, a protein that serves as a cofactor for certain LRR proteins. This is the first report of members of the LRR family with functional homologs in Pinus strobus and of a molecular basis for white pine blister rust resistance in Pinus strobus. |
| Databáze: | Directory of Open Access Journals |
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