HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: D500005-MCP200v1 4/11/1812    most recent Submit a response Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Glossary Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Lei, Z. Articles by Sumner, L. W. Search for Related Content PubMed PubMed Citation Articles by Lei, Z. Articles by Sumner, L. W. Social Bookmarking                      What's this?

Molecular & Cellular Proteomics 4:1812-1825, 2005.
© 2005 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Dataset

A Two-dimensional Electrophoresis Proteomic Reference Map and Systematic Identification of 1367 Proteins from a Cell Suspension Culture of the Model Legume Medicago truncatula^*,S

Zhentian Lei, Aaron M. Elmer, Bonnie S. Watson, Richard A. Dixon, Pedro J. Mendes and Lloyd W. Sumner^,¶

From the Plant Biology Division, The Samuel Roberts Noble Foundation, Ardmore, Oklahoma 73402 and the Virginia Bioinformatics Institute, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24061

The proteome of a Medicago truncatula cell suspension culture was analyzed using two-dimensional electrophoresis and nanoscale HPLC coupled to a tandem Q-TOF mass spectrometer (QSTAR Pulsar i) to yield an extensive protein reference map. Coomassie Brilliant Blue R-250 was used to visualize more than 1661 proteins, which were excised, subjected to in-gel trypsin digestion, and analyzed using nanoscale HPLC/MS/MS. The resulting spectral data were queried against a custom legume protein database using the MASCOT search engine. A total of 1367 of the 1661 proteins were identified with high rigor, yielding an identification success rate of 83% and 907 unique protein accession numbers. Functional annotation of the M. truncatula suspension cell proteins revealed a complete tricarboxylic acid cycle, a nearly complete glycolytic pathway, a significant portion of the ubiquitin pathway with the associated proteolytic and regulatory complexes, and many enzymes involved in secondary metabolism such as flavonoid/isoflavonoid, chalcone, and lignin biosynthesis. Proteins were also identified from most other functional classes including primary metabolism, energy production, disease/defense, protein destination/storage, protein synthesis, transcription, cell growth/division, and signal transduction. This work represents the most extensive proteomic description of M. truncatula suspension cells to date and provides a reference map for future comparative proteomic and functional genomic studies of the response of these cells to biotic and abiotic stress.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				E. Larrainzar, S. Wienkoop, W. Weckwerth, R. Ladrera, C. Arrese-Igor, and E. M. Gonzalez Medicago truncatula Root Nodule Proteome Analysis Reveals Differential Plant and Bacteroid Responses to Drought Stress Plant Physiology, July 1, 2007; 144(3): 1495 - 1507. [Abstract] [Full Text] [PDF]

				E. Urbanczyk-Wochniak and L. W. Sumner MedicCyc: a biochemical pathway database for Medicago truncatula Bioinformatics, June 1, 2007; 23(11): 1418 - 1423. [Abstract] [Full Text] [PDF]