Medina, M.L. and Haynes, P.A. and Breci, L. and Francisco, W.A. (2005) Analysis of secreted proteins from Aspergillus flavus. Proteomics, 5 (12). pp. 3153-3161.
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Abstract
MS/MS techniques in proteomics make possible the identification of proteins from organisms with little or no genome sequence information available. Peptide sequences are obtained from tandem mass spectra by matching peptide mass and fragmentation information to protein sequence information from related organisms, including unannotated genome sequence data. This peptide identification data can then be grouped and reconstructed into protein data. In this study, we have used this approach to study protein secretion by Aspergillus flavus, a filamentous fungus for which very little genome sequence information is available. A. flavus is capable of degrading the flavonoid rutin (quercetin 3-O-glycoside), as the only source of carbon via an extracellular enzyme system. In this continuing study, a proteomic analysis was used to identify secreted proteins from A. flavus when grown on rutin. The growth media glucose and potato dextrose were used to identify differentially expressed secreted proteins. The secreted proteins were analyzed by 1- and 2-DE and MS/MS. A total of 51 unique A. flavus secreted proteins were identified from the three growth conditions. Ten proteins were unique to rutin-, five to glucose- and one to potato dextrose-grown A. flavus. Sixteen secreted proteins were common to all three media. Fourteen identifications were of hypothetical proteins or proteins of unknown functions. To our knowledge, this is the first extensive proteomic study conducted to identify the secreted proteins from a filamentous fungus
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | Aspergillus flavus;Dispensable metabolic pathways;Rutin degradation;Secreted proteins;Tandem mass spectrometry |
| Author Affiliation: | Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ, USA |
| Subjects: | Plant Protection Crop Improvement Plant Physiology and Biochemistry > Biochemistry |
| Divisions: | General |
| Depositing User: | Ms Ishrath Durafsha |
| Date Deposited: | 26 Feb 2015 05:55 |
| Last Modified: | 26 Feb 2015 05:55 |
| Official URL: | http://dx.doi.org/10.1002/pmic.200401136 |
| URI: | http://eprints.icrisat.ac.in/id/eprint/13629 |
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