Plant Cell Applied Biosystems SYBR(R) Cells-to-CT(TM) Kits
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

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 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 ISI Web of Science (129)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Koehler, S. M.
Right arrow Articles by Ho, THD.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Koehler, S. M.
Right arrow Articles by Ho, THD.
Agricola
Right arrow Articles by Koehler, S. M.
Right arrow Articles by Ho, THD.

THE PLANT CELL, Vol 2, Issue 8 769-783, Copyright © 1990 by American Society of Plant Biologists

RESEARCH ARTICLES

Hormonal Regulation, Processing, and Secretion of Cysteine Proteinases in Barley Aleurone Layers

S. M. Koehler and THD. Ho
Department of Biology, Washington University, St. Louis, Missouri 63130

Barley aleurone layers synthesize and secrete several proteases in response to gibberellic acid (GA3). Two major cysteine proteinases designated EP-A (37,000 Mr) and EP-B (30,000 Mr) have been described [Koehler and Ho (1988). Plant Physiol. 87, 95-103]. We now report the cDNA cloning of EP-B and describe the post-translational processing and hormonal regulation of both cysteine proteinases. Three cDNAs for cysteine proteinases were cloned from GA3-induced barley aleurone layers. Genomic DNA gel blot analysis indicated that these are members of a small gene family with no more than four to five different genes. The proteins encoded by two of these clones, pHVEP1 and 4, are 98% similar to each other and are isozymes of EP-B. The proteins contain large preprosequences followed by the amino acid sequence described as the mature N terminus of purified EP-B, and are antigenic to EP-B antiserum. The results of pulse-chase experiments indicated that the post-translational processing of large prosequences proceeds in a multistep fashion to produce the mature enzymes. Processing intermediates for EP-B are observed both in the aleurone layers and surrounding incubation medium, but only mature EP-A is secreted. The regulation of synthesis of EP-A, EP-B, and other aleurone cysteine proteinases was compared at the protein and mRNA levels. We conclude that barley aleurone cysteine proteinases are differentially regulated with respect to their temporal and hormonally induced expression.


This article has been cited by other articles:


Home page
 Crop Sci.Home page
E. Herman
Soybean Allergenicity and Suppression of the Immunodominant Allergen
Crop Sci., January 31, 2005; 45(2): 462 - 467.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
M. Martinez, I. Rubio-Somoza, P. Carbonero, and I. Diaz
A cathepsin B-like cysteine protease gene from Hordeum vulgare (gene CatB) induced by GA in aleurone cells is under circadian control in leaves
J. Exp. Bot., March 1, 2003; 54(384): 951 - 959.
[Abstract] [Full Text] [PDF]

Home page
 Plant Cell PhysiolHome page
M. Taneyama, T. Okamoto, H. Yamane, and T. Minamikawa
Involvement of Gibberellins in Expression of a Cysteine Proteinase (SH-EP) in Cotyledons of Vigna mungo Seedlings
Plant Cell Physiol., November 1, 2001; 42(11): 1290 - 1293.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
K. Muntz, M.A. Belozersky, Y.E. Dunaevsky, A. Schlereth, and J. Tiedemann
Stored proteinases and the initiation of storage protein mobilization in seeds during germination and seedling growth
J. Exp. Bot., September 1, 2001; 52(362): 1741 - 1752.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
A. J. Kinney, R. Jung, and E. M. Herman
Cosuppression of the {{alpha}} Subunits of {beta}-Conglycinin in Transgenic Soybean Seeds Induces the Formation of Endoplasmic Reticulum-Derived Protein Bodies
PLANT CELL, May 1, 2001; 13(5): 1165 - 1178.
[Abstract] [Full Text]

Home page
 Plant Physiol.Home page
S.-L. Ho, W.-F. Tong, and S.-M. Yu
Multiple Mode Regulation of a Cysteine Proteinase Gene Expression in Rice
Plant Physiology, January 1, 2000; 122(1): 57 - 66.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Okomoto, T. Minamikawa, G. Edward, V. Vakharia, and E. Herman
Posttranslational Removal of the Carboxyl-terminal KDEL of the Cysteine Protease SH-EP Occurs Prior to Maturation of the Enzyme
J. Biol. Chem., April 16, 1999; 274(16): 11390 - 11398.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
A. Davy, I. Svendsen, S. O. Sørensen, M. Blom Sørensen, J. Rouster, M. Meldal, D. J. Simpson, and V. Cameron-Mills
Substrate Specificity of Barley Cysteine Endoproteases EP-A and EP-B
Plant Physiology, May 1, 1998; 117(1): 255 - 261.
[Abstract] [Full Text]

Home page
 JCBHome page
K. Toyooka, T. Okamoto, and T. Minamikawa
Cotyledon cells of Vigna mungo seedlings use at least two distinct autophagic machineries for degradation of starch granules and cellular components
J. Cell Biol., September 3, 2001; 154(5): 973 - 982.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications THE PLANT CELL PLANT PHYSIOLOGY
Copyright © 1990 by the American Society of Plant Biologists