Plant Physiol.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


First published online September 22, 2006; 10.1104/pp.106.086041

Plant Physiology 142:831-838 (2006)
© 2006 American Society of Plant Biologists

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
142/3/831    most recent
pp.106.086041v1
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 Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (16)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lease, K. A.
Right arrow Articles by Walker, J. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lease, K. A.
Right arrow Articles by Walker, J. C.
Agricola
Right arrow Articles by Lease, K. A.
Right arrow Articles by Walker, J. C.
GENOME ANALYSIS

The Arabidopsis Unannotated Secreted Peptide Database, a Resource for Plant Peptidomics[W]

Kevin A. Lease* and John C. Walker

Division of Biological Sciences, University of Missouri, Columbia, Missouri 65211

In the era of genomics, if a gene is not annotated, it is not investigated. Due to their small size, genes encoding peptides are often missed in genome annotations. Secreted peptides are important regulators of plant growth, development, and physiology. Identification of additional peptide signals by sequence homology searches has had limited success due to sequence heterogeneity. A bioinformatics approach was taken to find unannotated Arabidopsis (Arabidopsis thaliana) peptides. Arabidopsis chromosome sequences were searched for all open reading frames (ORFs) encoding peptides and small proteins between 25 and 250 amino acids in length. The translated ORFs were then sequentially queried for the presence of an amino-terminal cleavable signal peptide, the absence of transmembrane domains, and the absence of endoplasmic reticulum lumenal retention sequences. Next, the ORFs were filtered against the The Arabidopsis Information Resource 6.0 annotated Arabidopsis genes to remove those ORFs overlapping known genes. The remaining 33,809 ORFs were placed in a relational database to which additional annotation data were deposited. Genome-wide tiling array data were compared with the coordinates of the ORFs, supporting the possibility that many of the ORFs may be expressed. In addition, clustering and sequence similarity analyses revealed that many of the putative peptides are in gene families and/or appear to be present in the rice (Oryza sativa) genome. A subset of the ORFs was evaluated by reverse transcription-PCR and, for one-fifth of those, expression was detected. These results support the idea that the number and diversity of plant peptides is broader than currently assumed. The peptides identified and their annotation data may be viewed or downloaded through a searchable Web interface at peptidome.missouri.edu.


The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Kevin A. Lease (leasek{at}missouri.edu).

[W] The online version of this article contains Web-only data.

www.plantphysiol.org/cgi/doi/10.1104/pp.106.086041

* Corresponding author; e-mail leasek{at}missouri.edu; fax 573–884–9676.

Received July 11, 2006; accepted September 14, 2006; published September 22, 2006.




This article has been cited by other articles:


Home page
Plant Physiol.Home page
L. Zhang, L.-H. Tian, J.-F. Zhao, Y. Song, C.-J. Zhang, and Y. Guo
Identification of an Apoplastic Protein Involved in the Initial Phase of Salt Stress Response in Rice Root by Two-Dimensional Electrophoresis
Plant Physiology, February 1, 2009; 149(2): 916 - 928.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
Y. Amano, H. Tsubouchi, H. Shinohara, M. Ogawa, and Y. Matsubayashi
Tyrosine-sulfated glycopeptide involved in cellular proliferation and expansion in Arabidopsis
PNAS, November 13, 2007; 104(46): 18333 - 18338.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
C. A. Atkins and P. M. C. Smith
Translocation in Legumes: Assimilates, Nutrients, and Signaling Molecules
Plant Physiology, June 1, 2007; 144(2): 550 - 561.
[Full Text] [PDF]


Home page
Plant Physiol.Home page
A. P.M. Weber, K. L. Weber, K. Carr, C. Wilkerson, and J. B. Ohlrogge
Sampling the Arabidopsis Transcriptome with Massively Parallel Pyrosequencing
Plant Physiology, May 1, 2007; 144(1): 32 - 42.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 2006 by the American Society of Plant Biologists