Plant Physiol. Illumina
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 Google Scholar
Google Scholar
Right arrow Articles by Hammer, M. F.
Right arrow Articles by Sarath, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hammer, M. F.
Right arrow Articles by Sarath, G.
Agricola
Right arrow Articles by Hammer, M. F.
Right arrow Articles by Sarath, G.

PLANT PHYSIOLOGY , Vol 113, Issue 1 227-233, Copyright © 1997 by American Society of Plant Biologists

BIOCHEMISTRY AND ENZYMOLOGY

Purification of a Protein Phosphatase from Chloroplast Stroma Capable of Dephosphorylating the Light-Harvesting Complex-II

M. F. Hammer, J. Markwell and G. Sarath
Department of Biochemistry (M.H., J.M., G.S) and Center for Biotechnology (G.S.), University of Nebraska, Lincoln, Nebraska 68588-0664

A protein phosphatase was purified from the stroma of Pea (Pisum sativum L.) chloroplasts that is capable of dephosphorylating synthetic phosphopeptides. Following chromatographic purification of greater than 400-fold, two-dimensional electrophoresis indicated that the stromal protein phosphatase is a 29-kD protein. A similar molecular size was determined for the protein-phosphatase activity using gel-permeation chromatography, indicating that the stromal protein phosphatase is probably a monomer. The purified enzyme was able to dephosphorylate synthetic phosphopeptides, which mimic the thylakoid light-harvesting complex-II (LHC-II) N terminus, as well as LHC-II in thylakoid membranes, but did not dephosphorylate the major 64-kD phosphoprotein in the stroma. The stromal protein phosphatase did not discriminate between dephosphorylation of phosphothreonine and phosphoserine residues in synthetic peptide substrates, providing further evidence that this enzyme is distinct from the protein phosphatase localized in thylakoid membranes. The exact physiological role of the stromal protein phosphatase has yet to be determined, but it may function in the dephosphorylation of LHC-II.


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
M. Hansson, T. Dupuis, R. Stromquist, B. Andersson, A. V. Vener, and I. Carlberg
The Mobile Thylakoid Phosphoprotein TSP9 Interacts with the Light-harvesting Complex II and the Peripheries of Both Photosystems
J. Biol. Chem., June 1, 2007; 282(22): 16214 - 16222.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
E-M. Aro, M. Suorsa, A. Rokka, Y. Allahverdiyeva, V. Paakkarinen, A. Saleem, N. Battchikova, and E. Rintamaki
Dynamics of photosystem II: a proteomic approach to thylakoid protein complexes
J. Exp. Bot., January 1, 2005; 56(411): 347 - 356.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
M. Hansson and A. V. Vener
Identification of Three Previously Unknown in Vivo Protein Phosphorylation Sites in Thylakoid Membranes of Arabidopsis thaliana
Mol. Cell. Proteomics, August 1, 2003; 2(8): 550 - 559.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
I. Carlberg, M. Hansson, T. Kieselbach, W. P. Schroder, B. Andersson, and A. V. Vener
A novel plant protein undergoing light-induced phosphorylation and release from the photosynthetic thylakoid membranes
PNAS, January 21, 2003; 100(2): 757 - 762.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
A. Rokka, E.-M. Aro, R. G. Herrmann, B. Andersson, and A. V. Vener
Dephosphorylation of Photosystem II Reaction Center Proteins in Plant Photosynthetic Membranes as an Immediate Response to Abrupt Elevation of Temperature
Plant Physiology, August 1, 2000; 123(4): 1525 - 1536.
[Abstract] [Full Text]

Home page
 Proc. Natl. Acad. Sci. USAHome page
H. Zer, M. Vink, N. Keren, H. G. Dilly-Hartwig, H. Paulsen, R. G. Herrmann, B. Andersson, and I. Ohad
Regulation of thylakoid protein phosphorylation at the substrate level: Reversible light-induced conformational changes expose the phosphorylation site of the light-harvesting complex II
PNAS, July 6, 1999; 96(14): 8277 - 8282.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1997 by the American Society of Plant Biologists