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  Analysis of xylem sap proteins from Brassica napus

Kehr, J., Buhtz, A., & Giavalisco, P. (2005). Analysis of xylem sap proteins from Brassica napus. BMC Plant Biology, 5, 11. doi:10.1186/1471-2229-5-11.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-2BA2-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-2BA3-3
Genre: Journal Article

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 Creators:
Kehr, J.1, Author              
Buhtz, A.1, Author              
Giavalisco, P.2, Author              
Affiliations:
1Micro- and Protein-Analysis, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753346              
2Small Molecules, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753340              

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Free keywords: Brassica napus/*chemistry Cell Wall/metabolism/ultrastructure Electrophoresis, Gel, Two-Dimensional Lectins/analysis/classification/physiology Mass Spectrometry Peptide Hydrolases/analysis/classification/physiology Peroxidases/analysis/classification/physiology Plant Proteins/*analysis/classification/physiology Plant Stems/chemistry
 Abstract: Background: Substance transport in higher land plants is mediated by vascular bundles, consisting of phloem and xylem strands that interconnect all plant organs. While the phloem mainly allocates photoassimilates, the role of the xylem is the transport of water and inorganic nutrients from roots to all aerial plant parts. Only recently it was noticed that in addition to mineral salts, xylem sap contains organic nutrients and even proteins. Although these proteins might have important impact on the performance of above-ground organs, only a few of them have been identified so far and their physiological functions are still unclear. Results: We used root-pressure xylem exudate, collected from cut Brassica napus stems, to extract total proteins. These protein preparations were then separated by high-resolution two-dimensional gel electrophoresis (2-DE). After individual tryptic digests of the most abundant coomassie-stained protein spots, partial peptide sequence information was deduced from tandem mass spectrometric (MS/MS) fragmentation spectra and subsequently used for protein identifications by database searches. This approach resulted in the identification of 69 proteins. These identifications include different proteins potentially involved in defence-related reactions and cell wall metabolism. Conclusion: This study provides a comprehensive overview of the most abundant proteins present in xylem sap of Brassica napus. A number of 69 proteins could be identified from which many previously were not known to be localized to this compartment in any other plant species. Since Brassica napus, a close relative of the fully sequenced model plant Arabidopsis thaliana, was used as the experimental system, our results provide a large number of candidate proteins for directed molecular and biochemical analyses of the physiological functions of the xylem under different environmental and developmental conditions. This approach will allow exploiting many of the already established functional genomic resources, like i. e. the large mutant collections, that are available for Arabidopsis.

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Language(s): eng - English
 Dates: 2005-06-212005
 Publication Status: Published in print
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 Identifiers: ISI: ISI:000202935800001
DOI: 10.1186/1471-2229-5-11
ISSN: 1471-2229 (Electronic) 1471-2229 (Linking)
URI: ://000202935800001 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1182380/pdf/1471-2229-5-11.pdf
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Title: BMC Plant Biology
Source Genre: Journal
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Pages: - Volume / Issue: 5 Sequence Number: - Start / End Page: 11 Identifier: -