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


     


This Article
Right arrow Full Text
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 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 (31)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Moura, D. S.
Right arrow Articles by Ryan, C. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Moura, D. S.
Right arrow Articles by Ryan, C. A.
Agricola
Right arrow Articles by Moura, D. S.
Right arrow Articles by Ryan, C. A.

Plant Physiol, May 2001, Vol. 126, pp. 289-298

Wound-Inducible Proteinase Inhibitors in Pepper. Differential Regulation upon Wounding, Systemin, and Methyl Jasmonate1

Daniel S. Moura and Clarence A. Ryan*

Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340

Seven small (approximately 6,000 D) wound-inducible proteinase inhibitor proteins were isolated from leaves of pepper (Capsicum annuum) plants that are members of the potato inhibitor II family. N-terminal sequences obtained indicated that the pepper leaf proteinase inhibitors (PLPIs) exhibit homology to two GenBank accessions that code for preproteins containing three isoinhibitors domains each that, when post-translationally processed, can account for the mixture of isoinhibitors that are reported herein from pepper leaves. A constitutive level of PLPI proteins was found in pepper leaves, and these levels increased up to 2.6-fold upon wounding of the lower leaves. Exposing intact plants to methyl jasmonate vapors induced the accumulation of PLPIs. Supplying excised young pepper plants with water through the cut stems induced PLPI proteins to levels higher than those found in intact plants, but with high variability. Supplying the excised plants with systemin did not result in an increase of PLPI levels that were statistically higher than levels found in excised plants. Gel-blot analyses of PLPI induction revealed the presence of two mRNA bands, having slightly different mobilities in agarose gels. Only the low Mr mRNA is present in untreated control plants, and it appears to be responsible for the constitutive levels of PLPI found in leaves. Both mRNA species are wound- and methyl jasmonate-inducible. Only the low- Mr species is weakly induced by systemin, indicating a differential expression of the two PLPI species.


1 This research was supported in part by the Washington State University College of Agriculture Project 1791, by the National Science Foundation (grant nos. IBN-9184542 and IBN-9117795 to C.A.R.), and by the National Council for Scientific and Technologic Development graduate fellowship from the Brazilian Government (to D.S.M.).

* Corresponding author; e-mail cabudryan{at}hotmail.com; fax 509-335-7643.

© 2001 American Society of Plant Physiologists



This article has been cited by other articles:


Home page
ANN BOT (LOND)Home page
W.-M. Tian, S.-Q. Peng, X.-C. Wang, M.-J. Shi, Y.-Y. Chen, and Z.-H. Hu
Vegetative Storage Protein in Litchi chinensis, a Subtropical Evergreen Fruit Tree, Possesses Trypsin Inhibitor Activity
Ann. Bot., November 1, 2007; 100(6): 1199 - 1208.
[Abstract] [Full Text] [PDF]


Home page
J Exp BotHome page
K. Muntz
Protein dynamics and proteolysis in plant vacuoles
J. Exp. Bot., July 1, 2007; 58(10): 2391 - 2407.
[Abstract] [Full Text] [PDF]


Home page
GeneticsHome page
A. J. Heidel and X. Dong
Fitness Benefits of Systemic Acquired Resistance During Hyaloperonospora parasitica Infection in Arabidopsis thaliana
Genetics, July 1, 2006; 173(3): 1621 - 1628.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
M. Horn, A. G. Patankar, J. A. Zavala, J. Wu, L. Doleckova-Maresova, M. Vujtechova, M. Mares, and I. T. Baldwin
Differential Elicitation of Two Processing Proteases Controls the Processing Pattern of the Trypsin Proteinase Inhibitor Precursor in Nicotiana attenuata
Plant Physiology, September 1, 2005; 139(1): 375 - 388.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
J. A. Zavala, A. G. Patankar, K. Gase, D. Hui, and I. T. Baldwin
Manipulation of Endogenous Trypsin Proteinase Inhibitor Production in Nicotiana attenuata Demonstrates Their Function as Antiherbivore Defenses
Plant Physiology, March 1, 2004; 134(3): 1181 - 1190.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 2001 by the American Society of Plant Biologists