Skip Navigation

This Article
Right arrow Full Text (PDF)
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 Kinoshita, T.
Right arrow Articles by Hara-Nishimura, I.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kinoshita, T.
Right arrow Articles by Hara-Nishimura, I.
Agricola
Right arrow Articles by Kinoshita, T.
Right arrow Articles by Hara-Nishimura, I.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Plant and Cell Physiology, 1995, Vol. 36, No. 8 1555-1562
© 1995

The Sequence and Expression of the {gamma}-VPE Gene, One Member of a Family of Three Genes for Vacuolar Processing Enzymes in Arabidopsis thaliana

Tetsu Kinoshita1,2, Mikio Nishimura1,2 and Ikuko Hara-Nishimura1,2,3

1 Department of Cell Biology, National Institute for Basic Biology Okazaki, 444 Japan
2 Department of Molecular Biomechanics, School of Life Science, The Graduate University for Advanced Studies Okazaki, 444 Japan

3To whom correspondence should be addressed.

Vacuolar processing enzymes (VPEs) are responsible for the maturation of seed proteins. Southern blot analysis showed that a family of genes for VPEs in Arabidopsis thaliana was composed of three genes, for {alpha}-VPE, rß-VPE and {gamma}-VPE, respectively. The gene for {gamma}-VPE was isolated from a genomic library. It was composed of nine exons and eight introns. The positions of the introns were fully conserved among the three genes, with the exception that the {alpha}-VPE gene was missing the fifth intron found in the rß-VPE and {gamma}-VPE genes. The predicted {gamma}-VPE protein was 80% and 57% identical in terms of amino acid sequence to the {alpha}-VPE protein and rß-VPE protein, respectively. Northern blot analysis demonstrated that the {gamma}-VPE gene was expressed predominantly in the stems, with a lower level of expression in rosette and cauline leaves. However, the expression was not detected in roots, flowers plus buds, or green siliques, in contrast to the high-level expression of the rß-VPE gene in the flowers plus buds. Thus, {gamma}-VPE seems to be an isoform that is specific to vegetative organs. Members of the VPE family can be separated into two subfamilies, one that is specific to seeds and another that is specific to vegetative organs, such as leaves and stems. The members of the seed subfamily might function in the protein-storage vacuoles of seeds, while those of the vegetative subfamily might function in the lytic vacuoles of non-storage organs.

(Received May 17, 1995; Accepted September 18, 1995)
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
S. Nakaune, K. Yamada, M. Kondo, T. Kato, S. Tabata, M. Nishimura, and I. Hara-Nishimura
A Vacuolar Processing Enzyme, {delta}VPE, Is Involved in Seed Coat Formation at the Early Stage of Seed Development
PLANT CELL, March 1, 2005; 17(3): 876 - 887.
[Abstract] [Full Text] [PDF]


Home page
Plant CellHome page
D. Gruis, J. Schulze, and R. Jung
Storage Protein Accumulation in the Absence of the Vacuolar Processing Enzyme Family of Cysteine Proteases
PLANT CELL, January 1, 2004; 16(1): 270 - 290.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. Shimada, K. Yamada, M. Kataoka, S. Nakaune, Y. Koumoto, M. Kuroyanagi, S. Tabata, T. Kato, K. Shinozaki, M. Seki, et al.
Vacuolar Processing Enzymes Are Essential for Proper Processing of Seed Storage Proteins in Arabidopsis thaliana
J. Biol. Chem., August 22, 2003; 278(34): 32292 - 32299.
[Abstract] [Full Text] [PDF]


Home page
Plant CellHome page
D.(F. Gruis, D. A. Selinger, J. M. Curran, and R. Jung
Redundant Proteolytic Mechanisms Process Seed Storage Proteins in the Absence of Seed-Type Members of the Vacuolar Processing Enzyme Family of Cysteine Proteases
PLANT CELL, November 1, 2002; 14(11): 2863 - 2882.
[Abstract] [Full Text] [PDF]


Home page
Plant Cell PhysiolHome page
M. Kuroyanagi, M. Nishimura, and I. Hara-Nishimura
Activation of Arabidopsis Vacuolar Processing Enzyme by Self-Catalytic Removal of an Auto-Inhibitory Domain of the C-Terminal Propeptide
Plant Cell Physiol., February 1, 2002; 43(2): 143 - 151.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
K. Yamada, R. Matsushima, M. Nishimura, and I. Hara-Nishimura
A Slow Maturation of a Cysteine Protease with a Granulin Domain in the Vacuoles of Senescing Arabidopsis Leaves
Plant Physiology, December 1, 2001; 127(4): 1626 - 1634.
[Abstract] [Full Text] [PDF]


Home page
Plant Cell PhysiolHome page
Y. Hayashi, K. Yamada, T. Shimada, R. Matsushima, N. K. Nishizawa, M. Nishimura, and I. Hara-Nishimura
A Proteinase-Storing Body that Prepares for Cell Death or Stresses in the Epidermal Cells of Arabidopsis
Plant Cell Physiol., September 1, 2001; 42(9): 894 - 899.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. Yamada, T. Shimada, M. Kondo, M. Nishimura, and I. Hara-Nishimura
Multiple Functional Proteins Are Produced by Cleaving Asn-Gln Bonds of a Single Precursor by Vacuolar Processing Enzyme
J. Biol. Chem., January 22, 1999; 274(4): 2563 - 2570.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
C. Linnestad, D. N.P. Doan, R. C. Brown, B. E. Lemmon, D. J. Meyer, R. Jung, and O.-A. Olsen
Nucellain, a Barley Homolog of the Dicot Vacuolar-Processing Protease, Is Localized in Nucellar Cell Walls
Plant Physiology, December 1, 1998; 118(4): 1169 - 1180.
[Abstract] [Full Text]



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.