Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

Plant Physiology Preview
Published on April 29, 2009; 10.1104/pp.108.132415

OPEN ACCESS ARTICLE
This Article
Free via Open Access: OA
Right arrow Full Text (Plant Physiology Preview (PDF))
Right arrow Supplemental Data
Right arrowOA All Versions of this Article:
150/3/1160    most recent
pp.108.132415v1
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 (1)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kouri, E. D.
Right arrow Articles by Flemetakis, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kouri, E. D.
Right arrow Articles by Flemetakis, E.
Agricola
Right arrow Articles by Kouri, E. D.
Right arrow Articles by Flemetakis, E.

Received November 11, 2008
Accepted April 26, 2009

Molecular and Biochemical characterization of the Parvulin-type PPIases in Lotus japonicus

Evangelia D. Kouri , Nikolaos E. Labrou , Spiros D. Garbis , Katerina I. Kalliampakou , Catalina Stedel , Maria Dimou , Michael K. Udvardi , Panagiotis Katinakis , and Emmanouil Flemetakis *

Laboratory of Molecular Biology; Laboratory of Enzyme Technology; Department of Agricultural Biotechnology, Agricultural University of Athens, Iera Odos 75, 11855 Athens, Greece; Centre for Basic Research, Biomedical Research Foundation of the Academy of Athens, Soranou Ephessiou 4, 11527 Athens; The Samuel Roberts Noble Foundation, Plant Biology Division, 2510 Sam Noble Pky, Ardmore, OK 7340, USA

* Corresponding author; email: mflem{at}aua.gr.

The cis/trans isomerization of the peptide bond preceding proline is an intrinsically slow process, although important in many biological processes in both prokaryotes and eukaryotes. In vivo this isomerization is catalyzed by peptidyl-prolyl cis/trans isomerases (PPIases). Here we present the molecular and biochemical characterization of parvulin-type PPIase family members of the model legume Lotus japonicus, annotated as LjPar1, LjPar2 and LjPar3. Although LjPar1 and LjPar2 were found to be homologous to PIN1-type parvulins and hPar14 from human, respectively, LjPar3 represents a novel multi-domain parvulin, apparently present only in plants, which contains an active C-terminal sulfurtransferase domain. All Lotus parvulins were heterologously expressed and purified from Escherichia coli, and purified protein verification measurements where contacted an LC-MS based proteomic method. The biochemical characterization of the recombinant Lotus parvulins revealed that they posses PPIase activity towards synthetic tetrapeptides, although they exhibited different substrate specificities depending on the amino acid N-terminal to proline. These differences were also studied in a structural context using molecular modeling of the encoded polypeptides. Real-time RT-PCR revealed that the three parvulin genes of Lotus are ubiquitously expressed in all plant organs. LjPar1 was found to be upregulated during the later stages of nodule development. Subcellular localization of LjPar-eYFP fusions expressed in Arabidopsis leaf epidermal cells revealed that LjPar1- and LjPar2-eYFP fusions were localized in the cytoplasm and in the nucleus, in contrast to LjPar3-eYFP which was clearly localized in plastids. Divergent substrate specificities, expression profiles, and sub-cellular localization indicate that plant parvulin-type PPIases are probably involved in a wide range of biochemical and physiological processes.




This article has been cited by other articles:


Home page
 Plant Cell PhysiolHome page
B. Ingelsson, A. Shapiguzov, T. Kieselbach, and A. V. Vener
Peptidyl-Prolyl Isomerase Activity in Chloroplast Thylakoid Lumen is a Dispensable Function of Immunophilins in Arabidopsis thaliana
Plant Cell Physiol., October 1, 2009; 50(10): 1801 - 1814.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 2009 by the American Society of Plant Biologists