Skip Navigation



Plant and Cell Physiology Advance Access published online on January 19, 2005
Plant and Cell Physiology, doi:10.1093/pcp/pci002
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow All Versions of this Article:
46/1/87    most recent
pci002v1
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 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 arrowRequest Permissions
Google Scholar
Right arrow Articles by Bi, X.
Right arrow Articles by Bennett, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bi, X.
Right arrow Articles by Bennett, J.
Agricola
Right arrow Articles by Bi, X.
Right arrow Articles by Bennett, J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Plant and Cell Physiology 2005 © The Japanese Society of Plant Physiologists (JSPP); all rights researved.
Received March 8, 2004
Accepted October 8, 2004

Regular Paper

The Rice Nucellin Gene Orthologue, OsAsp1 Which Encodes An Active Aspartic Protease without Plant-Specific Insert, Is Strongly Expressed in Early Embryo

Xuezhi Bi 1*, Gurdev S. Khush 1, and John Bennett 1

1 Plant Breeding, Genetics, and Biochemistry Division, International Rice Research Institute, DAPO Box 7777, Metro Manila, Philippines

* To whom correspondence should be addressed.
Xuezhi Bi, E-mail: dbsbixz{at}nus.edu.sg


  Abstract

Barley nucellin gene was first reported to be nucellus-specific expression and play a role in the programmed cell death of the nucellus as an aspartic protease. In order to validate its specific expression and function, the rice orthologue, termed it OsAsp1, encoding a putative aspartic protease, was cloned and characterized. Temporal and spatial expression profile by northern blot, RT-PCR and in situ hybridization showed that OsAsp1 is most abundantly expressed in zygotic embryos 1-2 days after fertilization. It is also expressed in pollen, nucellus, ovary wall, shoot and root meristem and coleoptiles of immature seeds, and somatic embryos. Similar study in barley also showed that nucellin gene was not only expressed in barley nucellus but also strongly in embryos. Thus the protein name of nucellin should be re-assessed. Recombinant protein proOsAsp1 expressed in bacterium can be refolded and autolyzed at acidic pH 3.5 in vitro, and the mature peptide displayed protease activity. Nucellin has 3 close homologues in rice chromosome 11 and 12, Arabidopsis chromosomes 1 and 4 respectively. Unlike the typical plant aspartic protease, they compose the new class of aspartic protease without plant-specific insert in both monocot and dicot plant, whose function remains to be further explored.

Keywords: aspartic protease; gene expression; rice (Oryza sativa L.); embryo; recombinant protein.
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
 Proc. Natl. Acad. Sci. USAHome page
J. Chen, J. Ding, Y. Ouyang, H. Du, J. Yang, K. Cheng, J. Zhao, S. Qiu, X. Zhang, J. Yao, et al.
From the Cover: A triallelic system of S5 is a major regulator of the reproductive barrier and compatibility of indica-japonica hybrids in rice
PNAS, August 12, 2008; 105(32): 11436 - 11441.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
I. Simoes, R. Faro, D. Bur, and C. Faro
Characterization of Recombinant CDR1, an Arabidopsis Aspartic Proteinase Involved in Disease Resistance
J. Biol. Chem., October 26, 2007; 282(43): 31358 - 31365.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
L. Lombardi, S. Casani, N. Ceccarelli, L. Galleschi, P. Picciarelli, and R. Lorenzi
Programmed cell death of the nucellus during Sechium edule Sw. seed development is associated with activation of caspase-like proteases
J. Exp. Bot., August 28, 2007; (2007) erm137v1.
[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.