JXB Advance Access published online on April 4, 2006
Journal of Experimental Botany, doi:10.1093/jxb/erj156
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
1 Department of Plant and Microbial Biology, University of California, 111 Koshland Hall, Berkeley, CA 94720, USA; US Department of Agriculture, Agricultural Research Service, Western Regional Research Center, Albany, CA 94710, USA
* To whom correspondence should be addressed. By contrast to chloroplasts, our knowledge of amyloplasts--organelles that synthesize and store starch in heterotrophic plant tissues--is in a formative stage. While our understanding of what is considered their primary function, i.e. the biosynthesis and degradation of starch, has increased dramatically in recent years, relatively little is known about other biochemical processes taking place in these organelles. To help fill this gap, a proteomic analysis of amyloplasts isolated from the starchy endosperm of wheat seeds (10 d post-anthesis) has been conducted. The study has led to the identification of 289 proteins that function in a range of processes, including carbohydrate metabolism, cytoskeleton/plastid division, energetics, nitrogen and sulphur metabolism, nucleic acid-related reactions, synthesis of various building blocks, protein-related reactions, transport, signalling, stress, and a variety of other activities grouped under ‘miscellaneous’. The function of 12% of the proteins was unknown. The results highlight the role of the amyloplast as a starch-storing organelle that fulfills a spectrum of biosynthetic needs of the parent tissue. When compared with a recent proteomic analysis of whole endosperm, the current study demonstrates the advantage of using isolated organelles in proteomic studies. *Disclaimer: The mention of a trademark or proprietary product does not constitute a guarantee or warranty of the product by the United States Department of Agriculture and does not imply its approval to the exclusion of other products that may be suitable.
Received April 10, 2005
Accepted February 7, 2006
Plant Proteomics Special Issue Article
Proteome of amyloplasts isolated from developing wheat endosperm presents evidence of broad metabolic capability*
Yves Balmer 1,
William H. Vensel 2,
Frances M. DuPont 2,
Bob B. Buchanan 3 *,
and
William J. Hurkman 2
2 US Department of Agriculture, Agricultural Research Service, Western Regional Research Center, Albany, CA 94710, USA
3 Department of Plant and Microbial Biology, University of California, 111 Koshland Hall, Berkeley, CA 94720, USA
Bob B. Buchanan, E-mail: view{at}nature.berkeley.edu
Abstract
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  J. de Dios Barajas-Lopez, A. J. Serrato, A. Olmedilla, A. Chueca, and M. Sahrawy Localization in Roots and Flowers of Pea Chloroplastic Thioredoxin f and Thioredoxin m Proteins Reveals New Roles in Nonphotosynthetic Organs Plant Physiology, November 1, 2007; 145(3): 946 - 960. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 E. Lopez-Juez Plastid biogenesis, between light and shadows J. Exp. Bot., January 1, 2007; 58(1): 11 - 26. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. A. Siddique, J. Grossmann, W. Gruissem, and S. Baginsky Proteome Analysis of Bell Pepper (Capsicum annuum L.) Chromoplasts Plant Cell Physiol., December 1, 2006; 47(12): 1663 - 1673. [Abstract] [Full Text] [PDF]
|
|