Cargando…

Analysis of xylem sap proteins from Brassica napus

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Kehr, Julia, Buhtz, Anja, Giavalisco, Patrick
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1182380/
https://www.ncbi.nlm.nih.gov/pubmed/15969751
http://dx.doi.org/10.1186/1471-2229-5-11
_version_ 1782124664879841280
author Kehr, Julia
Buhtz, Anja
Giavalisco, Patrick
author_facet Kehr, Julia
Buhtz, Anja
Giavalisco, Patrick
author_sort Kehr, Julia
collection PubMed
description 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.
format Text
id pubmed-1182380
institution National Center for Biotechnology Information
language English
publishDate 2005
publisher BioMed Central
record_format MEDLINE/PubMed
spelling pubmed-11823802005-08-04 Analysis of xylem sap proteins from Brassica napus Kehr, Julia Buhtz, Anja Giavalisco, Patrick BMC Plant Biol Research Article 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. BioMed Central 2005-06-21 /pmc/articles/PMC1182380/ /pubmed/15969751 http://dx.doi.org/10.1186/1471-2229-5-11 Text en Copyright © 2005 Kehr et al; licensee BioMed Central Ltd.
spellingShingle Research Article
Kehr, Julia
Buhtz, Anja
Giavalisco, Patrick
Analysis of xylem sap proteins from Brassica napus
title Analysis of xylem sap proteins from Brassica napus
title_full Analysis of xylem sap proteins from Brassica napus
title_fullStr Analysis of xylem sap proteins from Brassica napus
title_full_unstemmed Analysis of xylem sap proteins from Brassica napus
title_short Analysis of xylem sap proteins from Brassica napus
title_sort analysis of xylem sap proteins from brassica napus
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1182380/
https://www.ncbi.nlm.nih.gov/pubmed/15969751
http://dx.doi.org/10.1186/1471-2229-5-11
work_keys_str_mv AT kehrjulia analysisofxylemsapproteinsfrombrassicanapus
AT buhtzanja analysisofxylemsapproteinsfrombrassicanapus
AT giavaliscopatrick analysisofxylemsapproteinsfrombrassicanapus