Skip Navigation


Plant and Cell Physiology Advance Access originally published online on April 8, 2005
Plant and Cell Physiology 2005 46(6):858-869; doi:10.1093/pcp/pci091
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
46/6/858    most recent
pci091v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (16)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Asatsuma, S.
Right arrow Articles by Mitsui, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Asatsuma, S.
Right arrow Articles by Mitsui, T.
Agricola
Right arrow Articles by Asatsuma, S.
Right arrow Articles by Mitsui, T.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

JSPP © 2005

Involvement of {alpha}-Amylase I-1 in Starch Degradation in Rice Chloroplasts

Satoru Asatsuma1, Chihoko Sawada1, Kimiko Itoh1, Mitsutoshi Okito2, Aya Kitajima2 and Toshiaki Mitsui1,2,3

1 Laboratories of Plant and Microbial Genome Control, Graduate School of Science and Technology, Niigata University, Niigata, 950-2181 Japan
2 Department of Applied Biological Chemistry, Niigata University, Niigata, 950-2181 Japan

3 Corresponding author: E-mail, t.mitsui{at}agr.niigata-u.ac.jp; Fax, +81-25-262-6641.

To determine the role of {alpha}-amylase isoform I-1 in the degradation of starch in rice leaf chloroplasts, we generated a series of transgenic rice plants with suppressed expression or overexpression of {alpha}-amylase I-1. In the lines with suppressed expression of {alpha}-amylase I-1 at both the mRNA and protein levels, seed germination and seedling growth were markedly delayed in comparison with those in the wild-type plants. However, the growth retardation was overcome by supplementation of sugars. Interestingly, a significant increase of starch accumulation in the young leaf tissues was observed under a sugar-supplemented condition. In contrast, the starch content of leaves was reduced in the plants overexpressing {alpha}-amylase I-1. In immunocytochemical analysis with specific anti-{alpha}-amylase I-1 antiserum, immuno-gold particles deposited in the chloroplasts and extracellular space in young leaf cells. We further examined the expression and targeting of {alpha}-amylase I-1 fused with the green fluorescent protein in re-differentiated green cells, and showed that the fluorescence of the expressed fusion protein co-localized with the chlorophyll autofluorescence in the transgenic cells. In addition, mature protein species of {alpha}-amylase I-1 bearing an oligosaccharide side chain were detected in the isolated chloroplasts. Based on these results, we concluded that {alpha}-amylase I-1 targets the chloroplasts through the endoplasmic reticulum–Golgi system and plays a significant role in the starch degradation in rice leaves.

(Received December 9, 2004; Accepted March 18, 2005)
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
Plant CellHome page
A. Kitajima, S. Asatsuma, H. Okada, Y. Hamada, K. Kaneko, Y. Nanjo, Y. Kawagoe, K. Toyooka, K. Matsuoka, M. Takeuchi, et al.
The Rice {alpha}-Amylase Glycoprotein Is Targeted from the Golgi Apparatus through the Secretory Pathway to the Plastids
PLANT CELL, September 1, 2009; 21(9): 2844 - 2858.
[Abstract] [Full Text] [PDF]


Home page
J Exp BotHome page
L. Moeller, Q. Gan, and K. Wang
A bacterial signal peptide is functional in plants and directs proteins to the secretory pathway
J. Exp. Bot., August 1, 2009; 60(12): 3337 - 3352.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
V. V. Radchuk, L. Borisjuk, N. Sreenivasulu, K. Merx, H.-P. Mock, H. Rolletschek, U. Wobus, and W. Weschke
Spatiotemporal Profiling of Starch Biosynthesis and Degradation in the Developing Barley Grain
Plant Physiology, May 1, 2009; 150(1): 190 - 204.
[Abstract] [Full Text] [PDF]


Home page
Plant CellHome page
D. C. Fulton, M. Stettler, T. Mettler, C. K. Vaughan, J. Li, P. Francisco, M. Gil, H. Reinhold, S. Eicke, G. Messerli, et al.
{beta}-AMYLASE4, a Noncatalytic Protein Required for Starch Breakdown, Acts Upstream of Three Active {beta}-Amylases in Arabidopsis Chloroplasts
PLANT CELL, April 1, 2008; 20(4): 1040 - 1058.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
H. Yamakawa, T. Hirose, M. Kuroda, and T. Yamaguchi
Comprehensive Expression Profiling of Rice Grain Filling-Related Genes under High Temperature Using DNA Microarray
Plant Physiology, May 1, 2007; 144(1): 258 - 277.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
A. K. Grennan
Regulation of Starch Metabolism in Arabidopsis Leaves
Plant Physiology, December 1, 2006; 142(4): 1343 - 1345.
[Full Text] [PDF]


Home page
Plant CellHome page
Y. Nanjo, H. Oka, N. Ikarashi, K. Kaneko, A. Kitajima, T. Mitsui, F. J. Munoz, M. Rodriguez-Lopez, E. Baroja-Fernandez, and J. Pozueta-Romero
Rice Plastidial N-Glycosylated Nucleotide Pyrophosphatase/Phosphodiesterase Is Transported from the ER-Golgi to the Chloroplast through the Secretory Pathway
PLANT CELL, October 1, 2006; 18(10): 2582 - 2592.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. Delatte, M. Umhang, M. Trevisan, S. Eicke, D. Thorneycroft, S. M. Smith, and S. C. Zeeman
Evidence for Distinct Mechanisms of Starch Granule Breakdown in Plants
J. Biol. Chem., April 28, 2006; 281(17): 12050 - 12059.
[Abstract] [Full Text] [PDF]


Home page
Plant Cell PhysiolHome page
J. Fettke, S. Poeste, N. Eckermann, A. Tiessen, M. Pauly, P. Geigenberger, and M. Steup
Analysis of Cytosolic Heteroglycans from Leaves of Transgenic Potato (Solanum tuberosum L.) Plants that Under- or Overexpress the Pho 2 Phosphorylase Isozyme
Plant Cell Physiol., December 1, 2005; 46(12): 1987 - 2004.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.