Plant Cell Tips for Better Browsing
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

Plant Cell Advance Online Publication
Published on February 18, 2005; 10.1105/tpc.104.028886

This Article
Right arrow Full Text - TPC Advance Online Pub. (PDF)
Right arrow All Versions of this Article:
17/3/849    most recent
tpc.104.028886v1
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 Google Scholar
Google Scholar
Right arrow Articles by Di Matteo, A.
Right arrow Articles by Tsernoglou, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Di Matteo, A.
Right arrow Articles by Tsernoglou, D.
Agricola
Right arrow Articles by Di Matteo, A.
Right arrow Articles by Tsernoglou, D.

Received October 27, 2004
Accepted December 28, 2004

Structural Basis for the Interaction between Pectin Methylesterase and a Specific Inhibitor Protein

Adele Di Matteo 1, Alfonso Giovane 2, Alessandro Raiola 3, Laura Camardella 4, Daniele Bonivento 5, Giulia De Lorenzo 2, Felice Cervone 3, Daniela Bellincampi 3*, and Demetrius Tsernoglou 5

1 Department of Biochemical Sciences, University of Rome, 00185 Rome, Italy; Department of Plant Biology, University of Rome, 00185 Rome, Italy
2 Department of Biochemistry and Biophysics, Second University of Naples, I-80138, Naples, Italy
3 Department of Plant Biology, University of Rome, 00185 Rome, Italy
4 Institute of Protein Biochemistry, Consiglio Nazionale delle Ricerche, I-80125, Naples, Italy
5 Department of Biochemical Sciences, University of Rome, 00185 Rome, Italy

* To whom correspondence should be addressed. E-mail: daniela.bellincampi{at}uniroma1.it.

Pectin, one of the main components of the plant cell wall, is secreted in a highly methyl-esterified form and subsequently deesterified in muro by pectin methylesterases (PMEs). In many developmental processes, PMEs are regulated by either differential expression or posttranslational control by protein inhibitors (PMEIs). PMEIs are typically active against plant PMEs and ineffective against microbial enzymes. Here, we describe the three-dimensional structure of the complex between the most abundant PME isoform from tomato fruit (Lycopersicon esculentum) and PMEI from kiwi (Actinidia deliciosa) at 1.9-Å resolution. The enzyme folds into a right-handed parallel {beta}-helical structure typical of pectic enzymes. The inhibitor is almost all helical, with four long {alpha}-helices aligned in an antiparallel manner in a classical up-and-down four-helical bundle. The two proteins form a stoichiometric 1:1 complex in which the inhibitor covers the shallow cleft of the enzyme where the putative active site is located. The four-helix bundle of the inhibitor packs roughly perpendicular to the main axis of the parallel {beta}-helix of PME, and three helices of the bundle interact with the enzyme. The interaction interface displays a polar character, typical of nonobligate complexes formed by soluble proteins. The structure of the complex gives an insight into the specificity of the inhibitor toward plant PMEs and the mechanism of regulation of these enzymes.




This article has been cited by other articles:


Home page
 J Exp BotHome page
M. Gonzalez-Aguero, L. Pavez, F. Ibanez, I. Pacheco, R. Campos-Vargas, L. A. Meisel, A. Orellana, J. Retamales, H. Silva, M. Gonzalez, et al.
Identification of woolliness response genes in peach fruit after post-harvest treatments
J. Exp. Bot., May 3, 2008; (2008) ern069v1.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
A. Siedlecka, S. Wiklund, M.-A. Peronne, F. Micheli, J. Lesniewska, I. Sethson, U. Edlund, L. Richard, B. Sundberg, and E. J. Mellerowicz
Pectin Methyl Esterase Inhibits Intrusive and Symplastic Cell Growth in Developing Wood Cells of Populus
Plant Physiology, February 1, 2008; 146(2): 554 - 565.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
V. Lionetti, A. Raiola, L. Camardella, A. Giovane, N. Obel, M. Pauly, F. Favaron, F. Cervone, and D. Bellincampi
Overexpression of Pectin Methylesterase Inhibitors in Arabidopsis Restricts Fungal Infection by Botrytis cinerea
Plant Physiology, April 1, 2007; 143(4): 1871 - 1880.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
W.-S. Jung, C.-K. Hong, S. Lee, C.-S. Kim, S.-J. Kim, S.-I. Kim, and S. Rhee
Structural and Functional Insights into Intramolecular Fructosyl Transfer by Inulin Fructotransferase
J. Biol. Chem., March 16, 2007; 282(11): 8414 - 8423.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
K. E. Francis, S. Y. Lam, and G. P. Copenhaver
Separation of Arabidopsis Pollen Tetrads Is Regulated by QUARTET1, a Pectin Methylesterase Gene
Plant Physiology, November 1, 2006; 142(3): 1004 - 1013.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
M. Bosch and P. K. Hepler
Pectin Methylesterases and Pectin Dynamics in Pollen Tubes
PLANT CELL, December 1, 2005; 17(12): 3219 - 3226.
[Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
ASPB Publications THE PLANT CELL PLANT PHYSIOLOGY
Copyright © 2005 by the American Society of Plant Biologists