Chloroplast proteomics: potentials and challenges
With the available Arabidopsis genome and near-completion of the rice genome sequencing project, large-scale analysis of plant proteins with mass spectrometry has now become possible. Determining the proteome of a cell is a challenging task, which is complicated by proteome dynamics and complexity....
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Published in | Journal of experimental botany Vol. 55; no. 400; pp. 1213 - 1220 |
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Main Authors | , |
Format | Journal Article Conference Proceeding |
Language | English |
Published |
Oxford
Oxford University Press
01.05.2004
Oxford Publishing Limited (England) |
Subjects | |
Online Access | Get full text |
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Summary: | With the available Arabidopsis genome and near-completion of the rice genome sequencing project, large-scale analysis of plant proteins with mass spectrometry has now become possible. Determining the proteome of a cell is a challenging task, which is complicated by proteome dynamics and complexity. The biochemical heterogeneity of proteins constrains the use of standardized analytical procedures and requires demanding techniques for proteome analysis. Several proteome studies of plant cell organelles have been reported, including chloroplasts and mitochondria. Chloroplasts are of particular interest for plant biologists because of their complex biochemical pathways for essential metabolic functions. Information from the chloroplast proteome will therefore provide new insights into pathway compartmentalization and protein sorting. Some approaches for the analysis of the chloroplast proteome and future prospects of plastid proteome research are discussed here. |
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Bibliography: | local:erh104 istex:AC0DA08F3A077D8DE372A3B5AA4A124428EDD9E8 To whom correspondence should be addressed. Fax: +41 1 632 10 79. E‐mail: sacha.baginsky@ipw.biol.ethz.ch ark:/67375/HXZ-3JB0NRRR-2 Received 24 September 2003; Accepted 19 January 2004 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 |
ISSN: | 0022-0957 1460-2431 |
DOI: | 10.1093/jxb/erh104 |